[{"doi":"10.1021/acs.nanolett.9b01983","_id":"10622","author":[{"full_name":"Polshyn, Hryhoriy","first_name":"Hryhoriy","id":"edfc7cb1-526e-11ec-b05a-e6ecc27e4e48","orcid":"0000-0001-8223-8896","last_name":"Polshyn"},{"first_name":"Tyler","full_name":"Naibert, Tyler","last_name":"Naibert"},{"last_name":"Budakian","first_name":"Raffi","full_name":"Budakian, Raffi"}],"page":"5476-5482","quality_controlled":"1","arxiv":1,"intvolume":"        19","citation":{"chicago":"Polshyn, Hryhoriy, Tyler Naibert, and Raffi Budakian. “Manipulating Multivortex States in Superconducting Structures.” <i>Nano Letters</i>. American Chemical Society, 2019. <a href=\"https://doi.org/10.1021/acs.nanolett.9b01983\">https://doi.org/10.1021/acs.nanolett.9b01983</a>.","short":"H. Polshyn, T. Naibert, R. Budakian, Nano Letters 19 (2019) 5476–5482.","ista":"Polshyn H, Naibert T, Budakian R. 2019. Manipulating multivortex states in superconducting structures. Nano Letters. 19(8), 5476–5482.","apa":"Polshyn, H., Naibert, T., &#38; Budakian, R. (2019). Manipulating multivortex states in superconducting structures. <i>Nano Letters</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.nanolett.9b01983\">https://doi.org/10.1021/acs.nanolett.9b01983</a>","ama":"Polshyn H, Naibert T, Budakian R. Manipulating multivortex states in superconducting structures. <i>Nano Letters</i>. 2019;19(8):5476-5482. doi:<a href=\"https://doi.org/10.1021/acs.nanolett.9b01983\">10.1021/acs.nanolett.9b01983</a>","ieee":"H. Polshyn, T. Naibert, and R. Budakian, “Manipulating multivortex states in superconducting structures,” <i>Nano Letters</i>, vol. 19, no. 8. American Chemical Society, pp. 5476–5482, 2019.","mla":"Polshyn, Hryhoriy, et al. “Manipulating Multivortex States in Superconducting Structures.” <i>Nano Letters</i>, vol. 19, no. 8, American Chemical Society, 2019, pp. 5476–82, doi:<a href=\"https://doi.org/10.1021/acs.nanolett.9b01983\">10.1021/acs.nanolett.9b01983</a>."},"acknowledgement":"We are grateful to Nadya Mason, Taylor Hughes, and Alexey Bezryadin for useful discussions. This work was supported by the DOE Basic Energy Sciences under DE-SC0012649 and the Department of Physics and the Frederick Seitz Materials Research Laboratory Central Facilities at the University of Illinois.","external_id":{"pmid":["31246034"],"arxiv":["1905.06303"]},"publication":"Nano Letters","type":"journal_article","abstract":[{"text":"We demonstrate a method for manipulating small ensembles of vortices in multiply connected superconducting structures. A micron-size magnetic particle attached to the tip of a silicon cantilever is used to locally apply magnetic flux through the superconducting structure. By scanning the tip over the surface of the device and by utilizing the dynamical coupling between the vortices and the cantilever, a high-resolution spatial map of the different vortex configurations is obtained. Moving the tip to a particular location in the map stabilizes a distinct multivortex configuration. Thus, the scanning of the tip over a particular trajectory in space permits nontrivial operations to be performed, such as braiding of individual vortices within a larger vortex ensemble—a key capability required by many proposals for topological quantum computing.","lang":"eng"}],"day":"27","date_created":"2022-01-13T15:11:14Z","keyword":["mechanical engineering","condensed matter physics","general materials science","general chemistry","bioengineering"],"volume":19,"title":"Manipulating multivortex states in superconducting structures","main_file_link":[{"url":"https://arxiv.org/abs/1905.06303","open_access":"1"}],"language":[{"iso":"eng"}],"pmid":1,"scopus_import":"1","extern":"1","issue":"8","status":"public","year":"2019","oa_version":"Preprint","user_id":"ea97e931-d5af-11eb-85d4-e6957dddbf17","publication_identifier":{"eissn":["1530-6992"],"issn":["1530-6984"]},"article_processing_charge":"No","oa":1,"publisher":"American Chemical Society","article_type":"original","date_published":"2019-06-27T00:00:00Z","month":"06","date_updated":"2022-01-13T15:41:24Z","publication_status":"published"},{"oa":1,"article_number":"2697","article_processing_charge":"No","date_published":"2019-06-19T00:00:00Z","article_type":"original","month":"06","publication_status":"published","date_updated":"2021-01-12T08:19:03Z","publisher":"Springer Nature","year":"2019","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["2041-1723"]},"oa_version":"Published Version","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"volume":10,"title":"Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex","language":[{"iso":"eng"}],"main_file_link":[{"url":"https://doi.org/10.1038/s41467-019-10490-9","open_access":"1"}],"day":"19","abstract":[{"text":"Atomic-resolution structure determination is crucial for understanding protein function. Cryo-EM and NMR spectroscopy both provide structural information, but currently cryo-EM does not routinely give access to atomic-level structural data, and, generally, NMR structure determination is restricted to small (<30 kDa) proteins. We introduce an integrated structure determination approach that simultaneously uses NMR and EM data to overcome the limits of each of these methods. The approach enables structure determination of the 468 kDa large dodecameric aminopeptidase TET2 to a precision and accuracy below 1 Å by combining secondary-structure information obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large subunits, distance restraints from backbone amides and ILV methyl groups, and a 4.1 Å resolution EM map. The resulting structure exceeds current standards of NMR and EM structure determination in terms of molecular weight and precision. Importantly, the approach is successful even in cases where only medium-resolution cryo-EM data are available.","lang":"eng"}],"date_created":"2020-09-17T10:28:25Z","extern":"1","pmid":1,"author":[{"last_name":"Gauto","full_name":"Gauto, Diego F.","first_name":"Diego F."},{"last_name":"Estrozi","first_name":"Leandro F.","full_name":"Estrozi, Leandro F."},{"full_name":"Schwieters, Charles D.","first_name":"Charles D.","last_name":"Schwieters"},{"first_name":"Gregory","full_name":"Effantin, Gregory","last_name":"Effantin"},{"last_name":"Macek","full_name":"Macek, Pavel","first_name":"Pavel"},{"full_name":"Sounier, Remy","first_name":"Remy","last_name":"Sounier"},{"last_name":"Sivertsen","full_name":"Sivertsen, Astrid C.","first_name":"Astrid C."},{"full_name":"Schmidt, Elena","first_name":"Elena","last_name":"Schmidt"},{"first_name":"Rime","full_name":"Kerfah, Rime","last_name":"Kerfah"},{"full_name":"Mas, Guillaume","first_name":"Guillaume","last_name":"Mas"},{"last_name":"Colletier","first_name":"Jacques-Philippe","full_name":"Colletier, Jacques-Philippe"},{"first_name":"Peter","full_name":"Güntert, Peter","last_name":"Güntert"},{"last_name":"Favier","full_name":"Favier, Adrien","first_name":"Adrien"},{"last_name":"Schoehn","full_name":"Schoehn, Guy","first_name":"Guy"},{"first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda"},{"full_name":"Boisbouvier, Jerome","first_name":"Jerome","last_name":"Boisbouvier"}],"quality_controlled":"1","doi":"10.1038/s41467-019-10490-9","_id":"8405","publication":"Nature Communications","type":"journal_article","intvolume":"        10","citation":{"mla":"Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.” <i>Nature Communications</i>, vol. 10, 2697, Springer Nature, 2019, doi:<a href=\"https://doi.org/10.1038/s41467-019-10490-9\">10.1038/s41467-019-10490-9</a>.","ieee":"D. F. Gauto <i>et al.</i>, “Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex,” <i>Nature Communications</i>, vol. 10. Springer Nature, 2019.","ama":"Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. <i>Nature Communications</i>. 2019;10. doi:<a href=\"https://doi.org/10.1038/s41467-019-10490-9\">10.1038/s41467-019-10490-9</a>","apa":"Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-019-10490-9\">https://doi.org/10.1038/s41467-019-10490-9</a>","ista":"Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen AC, Schmidt E, Kerfah R, Mas G, Colletier J-P, Güntert P, Favier A, Schoehn G, Schanda P, Boisbouvier J. 2019. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 10, 2697.","short":"D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier, A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A. Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).","chicago":"Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin, Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.” <i>Nature Communications</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1038/s41467-019-10490-9\">https://doi.org/10.1038/s41467-019-10490-9</a>."},"external_id":{"pmid":["31217444"]}},{"title":"Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR","language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"volume":141,"abstract":[{"text":"Aromatic residues are located at structurally important sites of many proteins. Probing their interactions and dynamics can provide important functional insight but is challenging in large proteins. Here, we introduce approaches to characterize dynamics of phenylalanine residues using 1H-detected fast magic-angle spinning (MAS) NMR combined with a tailored isotope-labeling scheme. Our approach yields isolated two-spin systems that are ideally suited for artefact-free dynamics measurements, and allows probing motions effectively without molecular-weight limitations. The application to the TET2 enzyme assembly of ~0.5 MDa size, the currently largest protein assigned by MAS NMR, provides insights into motions occurring on a wide range of time scales (ps-ms). We quantitatively probe ring flip motions, and show the temperature dependence by MAS NMR measurements down to 100 K. Interestingly, favorable line widths are observed down to 100 K, with potential implications for DNP NMR. Furthermore, we report the first 13C R1ρ MAS NMR relaxation-dispersion measurements and detect structural excursions occurring on a microsecond time scale in the entry pore to the catalytic chamber and at a trimer interface that was proposed as exit pore. We show that the labeling scheme with deuteration at ca. 50 kHz MAS provides superior resolution compared to 100 kHz MAS experiments with protonated, uniformly 13C-labeled samples.","lang":"eng"}],"day":"14","date_created":"2020-09-17T10:29:00Z","extern":"1","pmid":1,"quality_controlled":"1","page":"11183-11195","author":[{"last_name":"Gauto","full_name":"Gauto, Diego F.","first_name":"Diego F."},{"full_name":"Macek, Pavel","first_name":"Pavel","last_name":"Macek"},{"first_name":"Alessandro","full_name":"Barducci, Alessandro","last_name":"Barducci"},{"first_name":"Hugo","full_name":"Fraga, Hugo","last_name":"Fraga"},{"first_name":"Audrey","full_name":"Hessel, Audrey","last_name":"Hessel"},{"last_name":"Terauchi","first_name":"Tsutomu","full_name":"Terauchi, Tsutomu"},{"first_name":"David","full_name":"Gajan, David","last_name":"Gajan"},{"last_name":"Miyanoiri","first_name":"Yohei","full_name":"Miyanoiri, Yohei"},{"full_name":"Boisbouvier, Jerome","first_name":"Jerome","last_name":"Boisbouvier"},{"last_name":"Lichtenecker","full_name":"Lichtenecker, Roman","first_name":"Roman"},{"last_name":"Kainosho","first_name":"Masatsune","full_name":"Kainosho, Masatsune"},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"doi":"10.1021/jacs.9b04219","_id":"8408","publication":"Journal of the American Chemical Society","type":"journal_article","citation":{"ieee":"D. F. Gauto <i>et al.</i>, “Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR,” <i>Journal of the American Chemical Society</i>, vol. 141, no. 28. American Chemical Society, pp. 11183–11195, 2019.","mla":"Gauto, Diego F., et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle Spinning NMR.” <i>Journal of the American Chemical Society</i>, vol. 141, no. 28, American Chemical Society, 2019, pp. 11183–95, doi:<a href=\"https://doi.org/10.1021/jacs.9b04219\">10.1021/jacs.9b04219</a>.","ama":"Gauto DF, Macek P, Barducci A, et al. Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR. <i>Journal of the American Chemical Society</i>. 2019;141(28):11183-11195. doi:<a href=\"https://doi.org/10.1021/jacs.9b04219\">10.1021/jacs.9b04219</a>","apa":"Gauto, D. F., Macek, P., Barducci, A., Fraga, H., Hessel, A., Terauchi, T., … Schanda, P. (2019). Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jacs.9b04219\">https://doi.org/10.1021/jacs.9b04219</a>","ista":"Gauto DF, Macek P, Barducci A, Fraga H, Hessel A, Terauchi T, Gajan D, Miyanoiri Y, Boisbouvier J, Lichtenecker R, Kainosho M, Schanda P. 2019. Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical Society. 141(28), 11183–11195.","short":"D.F. Gauto, P. Macek, A. Barducci, H. Fraga, A. Hessel, T. Terauchi, D. Gajan, Y. Miyanoiri, J. Boisbouvier, R. Lichtenecker, M. Kainosho, P. Schanda, Journal of the American Chemical Society 141 (2019) 11183–11195.","chicago":"Gauto, Diego F., Pavel Macek, Alessandro Barducci, Hugo Fraga, Audrey Hessel, Tsutomu Terauchi, David Gajan, et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle Spinning NMR.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2019. <a href=\"https://doi.org/10.1021/jacs.9b04219\">https://doi.org/10.1021/jacs.9b04219</a>."},"external_id":{"pmid":["31199882"]},"intvolume":"       141","article_processing_charge":"No","date_published":"2019-06-14T00:00:00Z","month":"06","article_type":"original","publication_status":"published","date_updated":"2021-01-12T08:19:04Z","publisher":"American Chemical Society","status":"public","year":"2019","issue":"28","publication_identifier":{"issn":["0002-7863","1520-5126"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Submitted Version"},{"status":"public","year":"2019","issue":"2","publication_identifier":{"issn":["0002-7863","1520-5126"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Submitted Version","article_processing_charge":"No","publication_status":"published","date_updated":"2021-01-12T08:19:07Z","month":"01","article_type":"original","date_published":"2019-01-08T00:00:00Z","publisher":"American Chemical Society","quality_controlled":"1","page":"858-869","author":[{"full_name":"Rovó, Petra","first_name":"Petra","last_name":"Rovó"},{"first_name":"Colin A.","full_name":"Smith, Colin A.","last_name":"Smith"},{"first_name":"Diego","full_name":"Gauto, Diego","last_name":"Gauto"},{"last_name":"de Groot","first_name":"Bert L.","full_name":"de Groot, Bert L."},{"full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda"},{"full_name":"Linser, Rasmus","first_name":"Rasmus","last_name":"Linser"}],"_id":"8413","doi":"10.1021/jacs.8b09258","type":"journal_article","publication":"Journal of the American Chemical Society","external_id":{"pmid":["30620186"]},"citation":{"short":"P. Rovó, C.A. Smith, D. Gauto, B.L. de Groot, P. Schanda, R. Linser, Journal of the American Chemical Society 141 (2019) 858–869.","chicago":"Rovó, Petra, Colin A. Smith, Diego Gauto, Bert L. de Groot, Paul Schanda, and Rasmus Linser. “Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2019. <a href=\"https://doi.org/10.1021/jacs.8b09258\">https://doi.org/10.1021/jacs.8b09258</a>.","ista":"Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. 2019. Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. 141(2), 858–869.","ama":"Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. <i>Journal of the American Chemical Society</i>. 2019;141(2):858-869. doi:<a href=\"https://doi.org/10.1021/jacs.8b09258\">10.1021/jacs.8b09258</a>","apa":"Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., &#38; Linser, R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jacs.8b09258\">https://doi.org/10.1021/jacs.8b09258</a>","ieee":"P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, and R. Linser, “Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques,” <i>Journal of the American Chemical Society</i>, vol. 141, no. 2. American Chemical Society, pp. 858–869, 2019.","mla":"Rovó, Petra, et al. “Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.” <i>Journal of the American Chemical Society</i>, vol. 141, no. 2, American Chemical Society, 2019, pp. 858–69, doi:<a href=\"https://doi.org/10.1021/jacs.8b09258\">10.1021/jacs.8b09258</a>."},"intvolume":"       141","language":[{"iso":"eng"}],"title":"Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques","volume":141,"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"date_created":"2020-09-17T10:29:50Z","abstract":[{"text":"NMR relaxation dispersion methods provide a holistic way to observe microsecond time-scale protein backbone motion both in solution and in the solid state. Different nuclei (1H and 15N) and different relaxation dispersion techniques (Bloch–McConnell and near-rotary-resonance) give complementary information about the amplitudes and time scales of the conformational dynamics and provide comprehensive insights into the mechanistic details of the structural rearrangements. In this paper, we exemplify the benefits of the combination of various solution- and solid-state relaxation dispersion methods on a microcrystalline protein (α-spectrin SH3 domain), for which we are able to identify and model the functionally relevant conformational rearrangements around the ligand recognition loop occurring on multiple microsecond time scales. The observed loop motions suggest that the SH3 domain exists in a binding-competent conformation in dynamic equilibrium with a sterically impaired ground-state conformation both in solution and in crystalline form. This inherent plasticity between the interconverting macrostates is compatible with a conformational-preselection model and provides new insights into the recognition mechanisms of SH3 domains.","lang":"eng"}],"day":"08","extern":"1","pmid":1},{"pmid":1,"extern":"1","scopus_import":"1","day":"29","abstract":[{"text":"Molecular motors are essential to the living, generating fluctuations that boost transport and assist assembly. Active colloids, that consume energy to move, hold similar potential for man-made materials controlled by forces generated from within. Yet, their use as a powerhouse in materials science lacks. Here we show a massive acceleration of the annealing of a monolayer of passive beads by moderate addition of self-propelled microparticles. We rationalize our observations with a model of collisions that drive active fluctuations and activate the annealing. The experiment is quantitatively compared with Brownian dynamic simulations that further unveil a dynamical transition in the mechanism of annealing. Active dopants travel uniformly in the system or co-localize at the grain boundaries as a result of the persistence of their motion. Our findings uncover the potential of internal activity to control materials and lay the groundwork for the rise of materials science beyond equilibrium.","lang":"eng"}],"date_created":"2021-02-02T13:43:36Z","title":"Activity-controlled annealing of colloidal monolayers","language":[{"iso":"eng"}],"file_date_updated":"2021-02-02T13:47:21Z","volume":10,"keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"citation":{"ieee":"S. Ramananarivo, E. Ducrot, and J. A. Palacci, “Activity-controlled annealing of colloidal monolayers,” <i>Nature Communications</i>, vol. 10, no. 1. Springer Nature, 2019.","mla":"Ramananarivo, Sophie, et al. “Activity-Controlled Annealing of Colloidal Monolayers.” <i>Nature Communications</i>, vol. 10, no. 1, 3380, Springer Nature, 2019, doi:<a href=\"https://doi.org/10.1038/s41467-019-11362-y\">10.1038/s41467-019-11362-y</a>.","ama":"Ramananarivo S, Ducrot E, Palacci JA. Activity-controlled annealing of colloidal monolayers. <i>Nature Communications</i>. 2019;10(1). doi:<a href=\"https://doi.org/10.1038/s41467-019-11362-y\">10.1038/s41467-019-11362-y</a>","apa":"Ramananarivo, S., Ducrot, E., &#38; Palacci, J. A. (2019). Activity-controlled annealing of colloidal monolayers. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-019-11362-y\">https://doi.org/10.1038/s41467-019-11362-y</a>","ista":"Ramananarivo S, Ducrot E, Palacci JA. 2019. Activity-controlled annealing of colloidal monolayers. Nature Communications. 10(1), 3380.","short":"S. Ramananarivo, E. Ducrot, J.A. Palacci, Nature Communications 10 (2019).","chicago":"Ramananarivo, Sophie, Etienne Ducrot, and Jérémie A Palacci. “Activity-Controlled Annealing of Colloidal Monolayers.” <i>Nature Communications</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1038/s41467-019-11362-y\">https://doi.org/10.1038/s41467-019-11362-y</a>."},"ddc":["530"],"external_id":{"pmid":["31358762"],"arxiv":["1909.07382"]},"arxiv":1,"intvolume":"        10","type":"journal_article","publication":"Nature Communications","doi":"10.1038/s41467-019-11362-y","_id":"9060","quality_controlled":"1","author":[{"last_name":"Ramananarivo","full_name":"Ramananarivo, Sophie","first_name":"Sophie"},{"first_name":"Etienne","full_name":"Ducrot, Etienne","last_name":"Ducrot"},{"id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d","first_name":"Jérémie A","full_name":"Palacci, Jérémie A","last_name":"Palacci","orcid":"0000-0002-7253-9465"}],"publisher":"Springer Nature","article_type":"original","date_published":"2019-07-29T00:00:00Z","month":"07","date_updated":"2023-02-23T13:47:59Z","publication_status":"published","article_processing_charge":"No","article_number":"3380","oa":1,"file":[{"success":1,"creator":"cziletti","content_type":"application/pdf","checksum":"70c6e5d6fbea0932b0669505ab6633ec","access_level":"open_access","file_size":2820337,"date_updated":"2021-02-02T13:47:21Z","relation":"main_file","file_name":"2019_NatureComm_Ramananarivo.pdf","date_created":"2021-02-02T13:47:21Z","file_id":"9061"}],"oa_version":"Published Version","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"publication_identifier":{"issn":["2041-1723"]},"user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","has_accepted_license":"1","status":"public","issue":"1","year":"2019"},{"publication_status":"published","date_updated":"2024-10-14T12:14:34Z","month":"02","date_published":"2018-02-13T00:00:00Z","article_type":"original","publisher":"Springer Nature","oa":1,"article_number":"641","article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"eissn":["2041-1723"]},"oa_version":"Published Version","year":"2018","status":"public","scopus_import":"1","extern":"1","pmid":1,"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"volume":9,"language":[{"iso":"eng"}],"main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-02715-6","open_access":"1"}],"related_material":{"link":[{"url":"https://doi.org/10.1038/s41467-018-03701-2","relation":"erratum"}]},"title":"Reversible chromism of spiropyran in the cavity of a flexible coordination cage","date_created":"2023-08-01T09:39:32Z","day":"13","abstract":[{"text":"Confining molecules to volumes only slightly larger than the molecules themselves can profoundly alter their properties. Molecular switches—entities that can be toggled between two or more forms upon exposure to an external stimulus—often require conformational freedom to isomerize. Therefore, placing these switches in confined spaces can render them non-operational. To preserve the switchability of these species under confinement, we work with a water-soluble coordination cage that is flexible enough to adapt its shape to the conformation of the encapsulated guest. We show that owing to its flexibility, the cage is not only capable of accommodating—and solubilizing in water—several light-responsive spiropyran-based molecular switches, but, more importantly, it also provides an environment suitable for the efficient, reversible photoisomerization of the bound guests. Our findings pave the way towards studying various molecular switching processes in confined environments.","lang":"eng"}],"publication":"Nature Communications","type":"journal_article","intvolume":"         9","external_id":{"pmid":["29440687"]},"citation":{"ama":"Samanta D, Galaktionova D, Gemen J, et al. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-017-02715-6\">10.1038/s41467-017-02715-6</a>","apa":"Samanta, D., Galaktionova, D., Gemen, J., Shimon, L. J. W., Diskin-Posner, Y., Avram, L., … Klajn, R. (2018). Reversible chromism of spiropyran in the cavity of a flexible coordination cage. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-02715-6\">https://doi.org/10.1038/s41467-017-02715-6</a>","ieee":"D. Samanta <i>et al.</i>, “Reversible chromism of spiropyran in the cavity of a flexible coordination cage,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018.","mla":"Samanta, Dipak, et al. “Reversible Chromism of Spiropyran in the Cavity of a Flexible Coordination Cage.” <i>Nature Communications</i>, vol. 9, 641, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-017-02715-6\">10.1038/s41467-017-02715-6</a>.","short":"D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L. Avram, P. Král, R. Klajn, Nature Communications 9 (2018).","chicago":"Samanta, Dipak, Daria Galaktionova, Julius Gemen, Linda J. W. Shimon, Yael Diskin-Posner, Liat Avram, Petr Král, and Rafal Klajn. “Reversible Chromism of Spiropyran in the Cavity of a Flexible Coordination Cage.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-017-02715-6\">https://doi.org/10.1038/s41467-017-02715-6</a>.","ista":"Samanta D, Galaktionova D, Gemen J, Shimon LJW, Diskin-Posner Y, Avram L, Král P, Klajn R. 2018. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. Nature Communications. 9, 641."},"author":[{"last_name":"Samanta","first_name":"Dipak","full_name":"Samanta, Dipak"},{"last_name":"Galaktionova","full_name":"Galaktionova, Daria","first_name":"Daria"},{"last_name":"Gemen","full_name":"Gemen, Julius","first_name":"Julius"},{"full_name":"Shimon, Linda J. W.","first_name":"Linda J. W.","last_name":"Shimon"},{"last_name":"Diskin-Posner","full_name":"Diskin-Posner, Yael","first_name":"Yael"},{"last_name":"Avram","first_name":"Liat","full_name":"Avram, Liat"},{"last_name":"Král","first_name":"Petr","full_name":"Král, Petr"},{"first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn"}],"quality_controlled":"1","_id":"13374","doi":"10.1038/s41467-017-02715-6"},{"publisher":"Wiley","publication_status":"published","date_updated":"2024-10-14T12:15:04Z","date_published":"2018-06-11T00:00:00Z","article_type":"original","month":"06","article_processing_charge":"No","oa":1,"oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"eissn":["1521-3773"],"issn":["1433-7851"]},"issue":"24","year":"2018","status":"public","pmid":1,"scopus_import":"1","extern":"1","date_created":"2023-08-01T09:40:16Z","day":"11","abstract":[{"text":"Confining organic molecules to the surfaces of inorganic nanoparticles can induce intermolecular interactions between them, which can affect the composition of the mixed self-assembled monolayers obtained by co-adsorption from solution of two different molecules. Two thiolated ligands (a dialkylviologen and a zwitterionic sulfobetaine) that can interact with each other electrostatically were coadsorbed onto gold nanoparticles. The nanoparticles favor a narrow range of ratios of these two molecules that is largely independent of the molar ratio in solution. Changing the solution molar ratio of the two ligands by a factor of 5 000 affects the on-nanoparticle ratio of these ligands by only threefold. This behavior is reminiscent of the formation of insoluble inorganic salts (such as AgCl), which similarly compensate positive and negative charges upon crystallizing. Our results pave the way towards developing well-defined hybrid organic–inorganic nanostructures.","lang":"eng"}],"volume":57,"keyword":["General Chemistry","Catalysis"],"language":[{"iso":"eng"}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1002/anie.201800673"}],"title":"“Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles","intvolume":"        57","external_id":{"pmid":["29673022"]},"citation":{"short":"Z. Chu, Y. Han, P. Král, R. Klajn, Angewandte Chemie International Edition 57 (2018) 7023–7027.","chicago":"Chu, Zonglin, Yanxiao Han, Petr Král, and Rafal Klajn. “‘Precipitation on Nanoparticles’: Attractive Intermolecular Interactions Stabilize Specific Ligand Ratios on the Surfaces of Nanoparticles.” <i>Angewandte Chemie International Edition</i>. Wiley, 2018. <a href=\"https://doi.org/10.1002/anie.201800673\">https://doi.org/10.1002/anie.201800673</a>.","ista":"Chu Z, Han Y, Král P, Klajn R. 2018. “Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles. Angewandte Chemie International Edition. 57(24), 7023–7027.","ama":"Chu Z, Han Y, Král P, Klajn R. “Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles. <i>Angewandte Chemie International Edition</i>. 2018;57(24):7023-7027. doi:<a href=\"https://doi.org/10.1002/anie.201800673\">10.1002/anie.201800673</a>","apa":"Chu, Z., Han, Y., Král, P., &#38; Klajn, R. (2018). “Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles. <i>Angewandte Chemie International Edition</i>. Wiley. <a href=\"https://doi.org/10.1002/anie.201800673\">https://doi.org/10.1002/anie.201800673</a>","ieee":"Z. Chu, Y. Han, P. Král, and R. Klajn, “‘Precipitation on nanoparticles’: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles,” <i>Angewandte Chemie International Edition</i>, vol. 57, no. 24. Wiley, pp. 7023–7027, 2018.","mla":"Chu, Zonglin, et al. “‘Precipitation on Nanoparticles’: Attractive Intermolecular Interactions Stabilize Specific Ligand Ratios on the Surfaces of Nanoparticles.” <i>Angewandte Chemie International Edition</i>, vol. 57, no. 24, Wiley, 2018, pp. 7023–27, doi:<a href=\"https://doi.org/10.1002/anie.201800673\">10.1002/anie.201800673</a>."},"type":"journal_article","publication":"Angewandte Chemie International Edition","_id":"13377","doi":"10.1002/anie.201800673","author":[{"full_name":"Chu, Zonglin","first_name":"Zonglin","last_name":"Chu"},{"last_name":"Han","first_name":"Yanxiao","full_name":"Han, Yanxiao"},{"last_name":"Král","first_name":"Petr","full_name":"Král, Petr"},{"first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn"}],"page":"7023-7027","quality_controlled":"1"},{"year":"2018","status":"public","oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["2041-1723"]},"article_number":"1806","article_processing_charge":"No","oa":1,"publisher":"Springer Nature","date_published":"2018-05-04T00:00:00Z","month":"05","article_type":"original","publication_status":"published","date_updated":"2023-11-07T11:46:12Z","doi":"10.1038/s41467-018-04139-2","_id":"14284","author":[{"last_name":"Bräuning","full_name":"Bräuning, Bastian","first_name":"Bastian"},{"last_name":"Bertosin","first_name":"Eva","full_name":"Bertosin, Eva"},{"last_name":"Praetorius","full_name":"Praetorius, Florian M","first_name":"Florian M","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62"},{"last_name":"Ihling","full_name":"Ihling, Christian","first_name":"Christian"},{"full_name":"Schatt, Alexandra","first_name":"Alexandra","last_name":"Schatt"},{"last_name":"Adler","first_name":"Agnes","full_name":"Adler, Agnes"},{"first_name":"Klaus","full_name":"Richter, Klaus","last_name":"Richter"},{"first_name":"Andrea","full_name":"Sinz, Andrea","last_name":"Sinz"},{"last_name":"Dietz","first_name":"Hendrik","full_name":"Dietz, Hendrik"},{"full_name":"Groll, Michael","first_name":"Michael","last_name":"Groll"}],"quality_controlled":"1","intvolume":"         9","citation":{"ista":"Bräuning B, Bertosin E, Praetorius FM, Ihling C, Schatt A, Adler A, Richter K, Sinz A, Dietz H, Groll M. 2018. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Nature Communications. 9, 1806.","short":"B. Bräuning, E. Bertosin, F.M. Praetorius, C. Ihling, A. Schatt, A. Adler, K. Richter, A. Sinz, H. Dietz, M. Groll, Nature Communications 9 (2018).","chicago":"Bräuning, Bastian, Eva Bertosin, Florian M Praetorius, Christian Ihling, Alexandra Schatt, Agnes Adler, Klaus Richter, Andrea Sinz, Hendrik Dietz, and Michael Groll. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>.","mla":"Bräuning, Bastian, et al. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>, vol. 9, 1806, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>.","ieee":"B. Bräuning <i>et al.</i>, “Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018.","ama":"Bräuning B, Bertosin E, Praetorius FM, et al. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>","apa":"Bräuning, B., Bertosin, E., Praetorius, F. M., Ihling, C., Schatt, A., Adler, A., … Groll, M. (2018). Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>"},"external_id":{"pmid":["29728606"]},"publication":"Nature Communications","type":"journal_article","day":"04","abstract":[{"lang":"eng","text":"Pore-forming toxins (PFT) are virulence factors that transform from soluble to membrane-bound states. The Yersinia YaxAB system represents a family of binary α-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures. YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the molecular basis for its two-component lytic mechanism remains elusive. Here, we present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy map of the YaxAB complex. Our structures reveal a pore predominantly composed of decamers of YaxA–YaxB heterodimers. Both subunits bear membrane-active moieties, but only YaxA is capable of binding to membranes by itself. YaxB can subsequently be recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices. Pore formation can progress by further oligomerization of YaxA–YaxB dimers. Our results allow for a comparison between pore assemblies belonging to the wider ClyA-like family of α-PFTs, highlighting diverse pore architectures."}],"date_created":"2023-09-06T12:07:33Z","volume":9,"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-018-04139-2"}],"language":[{"iso":"eng"}],"pmid":1,"extern":"1","scopus_import":"1"},{"doi":"10.1021/acs.chemmater.8b03108","_id":"15107","quality_controlled":"1","status":"public","author":[{"full_name":"Roy, Soumendu","first_name":"Soumendu","last_name":"Roy"},{"last_name":"Roy","orcid":"0000-0002-6883-4939","id":"67a1dc7d-cffb-11ee-b082-e15ca6a616d9","first_name":"Sumit","full_name":"Roy, Sumit"},{"full_name":"Rao, Anish","first_name":"Anish","last_name":"Rao"},{"last_name":"Devatha","full_name":"Devatha, Gayathri","first_name":"Gayathri"},{"full_name":"Pillai, Pramod P.","first_name":"Pramod P.","last_name":"Pillai"}],"page":"8415-8419","issue":"23","year":"2018","citation":{"short":"S. Roy, S. Roy, A. Rao, G. Devatha, P.P. Pillai, Chemistry of Materials 30 (2018) 8415–8419.","chicago":"Roy, Soumendu, Sumit Roy, Anish Rao, Gayathri Devatha, and Pramod P. Pillai. “Precise Nanoparticle–Reactant Interaction Outplays Ligand Poisoning in Visible-Light Photocatalysis.” <i>Chemistry of Materials</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acs.chemmater.8b03108\">https://doi.org/10.1021/acs.chemmater.8b03108</a>.","ista":"Roy S, Roy S, Rao A, Devatha G, Pillai PP. 2018. Precise nanoparticle–reactant interaction outplays ligand poisoning in visible-light photocatalysis. Chemistry of Materials. 30(23), 8415–8419.","ama":"Roy S, Roy S, Rao A, Devatha G, Pillai PP. Precise nanoparticle–reactant interaction outplays ligand poisoning in visible-light photocatalysis. <i>Chemistry of Materials</i>. 2018;30(23):8415-8419. doi:<a href=\"https://doi.org/10.1021/acs.chemmater.8b03108\">10.1021/acs.chemmater.8b03108</a>","apa":"Roy, S., Roy, S., Rao, A., Devatha, G., &#38; Pillai, P. P. (2018). Precise nanoparticle–reactant interaction outplays ligand poisoning in visible-light photocatalysis. <i>Chemistry of Materials</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.chemmater.8b03108\">https://doi.org/10.1021/acs.chemmater.8b03108</a>","mla":"Roy, Soumendu, et al. “Precise Nanoparticle–Reactant Interaction Outplays Ligand Poisoning in Visible-Light Photocatalysis.” <i>Chemistry of Materials</i>, vol. 30, no. 23, American Chemical Society, 2018, pp. 8415–19, doi:<a href=\"https://doi.org/10.1021/acs.chemmater.8b03108\">10.1021/acs.chemmater.8b03108</a>.","ieee":"S. Roy, S. Roy, A. Rao, G. Devatha, and P. P. Pillai, “Precise nanoparticle–reactant interaction outplays ligand poisoning in visible-light photocatalysis,” <i>Chemistry of Materials</i>, vol. 30, no. 23. American Chemical Society, pp. 8415–8419, 2018."},"oa_version":"None","intvolume":"        30","publication_identifier":{"issn":["0897-4756"],"eissn":["1520-5002"]},"type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Chemistry of Materials","day":"19","article_processing_charge":"No","date_created":"2024-03-12T12:54:30Z","title":"Precise nanoparticle–reactant interaction outplays ligand poisoning in visible-light photocatalysis","language":[{"iso":"eng"}],"volume":30,"keyword":["Materials Chemistry","General Chemical Engineering","General Chemistry"],"publisher":"American Chemical Society","date_published":"2018-11-19T00:00:00Z","month":"11","article_type":"review","date_updated":"2024-03-20T07:50:07Z","extern":"1","scopus_import":"1","publication_status":"published"},{"date_created":"2021-11-26T12:41:38Z","abstract":[{"lang":"eng","text":"Mapping free-energy landscapes has proved to be a powerful tool for studying reaction mechanisms. Many complex biomolecular assembly processes, however, have remained challenging to access using this approach, including the aggregation of peptides and proteins into amyloid fibrils implicated in a range of disorders. Here, we generalize the strategy used to probe free-energy landscapes in protein folding to determine the activation energies and entropies that characterize each of the molecular steps in the aggregation of the amyloid-β peptide (Aβ42), which is associated with Alzheimer’s disease. Our results reveal that interactions between monomeric Aβ42 and amyloid fibrils during fibril-dependent secondary nucleation fundamentally reverse the thermodynamic signature of this process relative to primary nucleation, even though both processes generate aggregates from soluble peptides. By mapping the energetic and entropic contributions along the reaction trajectories, we show that the catalytic efficiency of Aβ42 fibril surfaces results from the enthalpic stabilization of adsorbing peptides in conformations amenable to nucleation, resulting in a dramatic lowering of the activation energy for nucleation."}],"day":"26","keyword":["general chemical engineering","general chemistry"],"volume":10,"language":[{"iso":"eng"}],"title":"Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide","pmid":1,"extern":"1","scopus_import":"1","_id":"10360","doi":"10.1038/s41557-018-0023-x","author":[{"last_name":"Cohen","first_name":"Samuel I. A.","full_name":"Cohen, Samuel I. A."},{"last_name":"Cukalevski","full_name":"Cukalevski, Risto","first_name":"Risto"},{"last_name":"Michaels","first_name":"Thomas C. T.","full_name":"Michaels, Thomas C. T."},{"full_name":"Šarić, Anđela","first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","orcid":"0000-0002-7854-2139","last_name":"Šarić"},{"last_name":"Törnquist","full_name":"Törnquist, Mattias","first_name":"Mattias"},{"full_name":"Vendruscolo, Michele","first_name":"Michele","last_name":"Vendruscolo"},{"last_name":"Dobson","first_name":"Christopher M.","full_name":"Dobson, Christopher M."},{"first_name":"Alexander K.","full_name":"Buell, Alexander K.","last_name":"Buell"},{"full_name":"Knowles, Tuomas P. J.","first_name":"Tuomas P. J.","last_name":"Knowles"},{"last_name":"Linse","first_name":"Sara","full_name":"Linse, Sara"}],"page":"523-531","quality_controlled":"1","intvolume":"        10","external_id":{"pmid":["29581486"]},"citation":{"ista":"Cohen SIA, Cukalevski R, Michaels TCT, Šarić A, Törnquist M, Vendruscolo M, Dobson CM, Buell AK, Knowles TPJ, Linse S. 2018. Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. Nature Chemistry. 10(5), 523–531.","chicago":"Cohen, Samuel I. A., Risto Cukalevski, Thomas C. T. Michaels, Anđela Šarić, Mattias Törnquist, Michele Vendruscolo, Christopher M. Dobson, Alexander K. Buell, Tuomas P. J. Knowles, and Sara Linse. “Distinct Thermodynamic Signatures of Oligomer Generation in the Aggregation of the Amyloid-β Peptide.” <i>Nature Chemistry</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41557-018-0023-x\">https://doi.org/10.1038/s41557-018-0023-x</a>.","short":"S.I.A. Cohen, R. Cukalevski, T.C.T. Michaels, A. Šarić, M. Törnquist, M. Vendruscolo, C.M. Dobson, A.K. Buell, T.P.J. Knowles, S. Linse, Nature Chemistry 10 (2018) 523–531.","mla":"Cohen, Samuel I. A., et al. “Distinct Thermodynamic Signatures of Oligomer Generation in the Aggregation of the Amyloid-β Peptide.” <i>Nature Chemistry</i>, vol. 10, no. 5, Springer Nature, 2018, pp. 523–31, doi:<a href=\"https://doi.org/10.1038/s41557-018-0023-x\">10.1038/s41557-018-0023-x</a>.","ieee":"S. I. A. Cohen <i>et al.</i>, “Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide,” <i>Nature Chemistry</i>, vol. 10, no. 5. Springer Nature, pp. 523–531, 2018.","apa":"Cohen, S. I. A., Cukalevski, R., Michaels, T. C. T., Šarić, A., Törnquist, M., Vendruscolo, M., … Linse, S. (2018). Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. <i>Nature Chemistry</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41557-018-0023-x\">https://doi.org/10.1038/s41557-018-0023-x</a>","ama":"Cohen SIA, Cukalevski R, Michaels TCT, et al. Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. <i>Nature Chemistry</i>. 2018;10(5):523-531. doi:<a href=\"https://doi.org/10.1038/s41557-018-0023-x\">10.1038/s41557-018-0023-x</a>"},"acknowledgement":"We thank B. Jönsson and I. André for helpful discussions. We acknowledge financial support from the Schiff Foundation (S.I.A.C.), St John’s College, Cambridge (S.I.A.C.), the Royal Physiographic Society (R.C.), the Research School FLÄK of Lund University (S.L., R.C.), the Swedish Research Council (S.L.) and its Linneaus Centre Organizing Molecular Matter (S.L.), the Crafoord Foundation (S.L.), Alzheimerfonden (S.L.), the European Research Council (S.L.), NanoLund (S.L.), Knut and Alice Wallenberg Foundation (S.L.), Peterhouse, Cambridge (T.C.T.M.), the Swiss National Science Foundation (T.C.T.M.), Magdalene College, Cambridge (A.K.B.), the Leverhulme Trust (A.K.B.), the Royal Society (A.Š.), the Academy of Medical Sciences (A.Š.), the Wellcome Trust (C.M.D., T.P.J.K., A.Š.), and the Centre for Misfolding Diseases (C.M.D., T.P.J.K, M.V.). A.K.B. thanks the Alzheimer Forschung Initiative (AFI).","publication":"Nature Chemistry","type":"journal_article","article_processing_charge":"No","publisher":"Springer Nature","date_updated":"2021-11-26T15:14:00Z","publication_status":"published","month":"03","date_published":"2018-03-26T00:00:00Z","article_type":"original","year":"2018","issue":"5","status":"public","oa_version":"None","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","publication_identifier":{"eissn":["1755-4349"],"issn":["1755-4330"]}},{"doi":"10.1021/acs.chemrev.7b00570","_id":"8442","year":"2018","page":"3559-3607","status":"public","issue":"7","author":[{"full_name":"Chipot, Christophe","first_name":"Christophe","last_name":"Chipot"},{"first_name":"François","full_name":"Dehez, François","last_name":"Dehez"},{"last_name":"Schnell","first_name":"Jason R.","full_name":"Schnell, Jason R."},{"first_name":"Nicole","full_name":"Zitzmann, Nicole","last_name":"Zitzmann"},{"full_name":"Pebay-Peyroula, Eva","first_name":"Eva","last_name":"Pebay-Peyroula"},{"last_name":"Catoire","first_name":"Laurent J.","full_name":"Catoire, Laurent J."},{"full_name":"Miroux, Bruno","first_name":"Bruno","last_name":"Miroux"},{"last_name":"Kunji","first_name":"Edmund R. S.","full_name":"Kunji, Edmund R. S."},{"first_name":"Gianluigi","full_name":"Veglia, Gianluigi","last_name":"Veglia"},{"last_name":"Cross","full_name":"Cross, Timothy A.","first_name":"Timothy A."},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"quality_controlled":"1","intvolume":"       118","citation":{"short":"C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire, B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118 (2018) 3559–3607.","chicago":"Chipot, Christophe, François Dehez, Jason R. Schnell, Nicole Zitzmann, Eva Pebay-Peyroula, Laurent J. Catoire, Bruno Miroux, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.” <i>Chemical Reviews</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">https://doi.org/10.1021/acs.chemrev.7b00570</a>.","ista":"Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ, Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P. 2018. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. Chemical Reviews. 118(7), 3559–3607.","ama":"Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. <i>Chemical Reviews</i>. 2018;118(7):3559-3607. doi:<a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">10.1021/acs.chemrev.7b00570</a>","apa":"Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire, L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. <i>Chemical Reviews</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">https://doi.org/10.1021/acs.chemrev.7b00570</a>","mla":"Chipot, Christophe, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.” <i>Chemical Reviews</i>, vol. 118, no. 7, American Chemical Society, 2018, pp. 3559–607, doi:<a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">10.1021/acs.chemrev.7b00570</a>.","ieee":"C. Chipot <i>et al.</i>, “Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies,” <i>Chemical Reviews</i>, vol. 118, no. 7. American Chemical Society, pp. 3559–3607, 2018."},"oa_version":"None","type":"journal_article","publication":"Chemical Reviews","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["0009-2665","1520-6890"]},"abstract":[{"text":"Membrane proteins perform a host of vital cellular functions. Deciphering the molecular mechanisms whereby they fulfill these functions requires detailed biophysical and structural investigations. Detergents have proven pivotal to extract the protein from its native surroundings. Yet, they provide a milieu that departs significantly from that of the biological membrane, to the extent that the structure, the dynamics, and the interactions of membrane proteins in detergents may considerably vary, as compared to the native environment. Understanding the impact of detergents on membrane proteins is, therefore, crucial to assess the biological relevance of results obtained in detergents. Here, we review the strengths and weaknesses of alkyl phosphocholines (or foscholines), the most widely used detergent in solution-NMR studies of membrane proteins. While this class of detergents is often successful for membrane protein solubilization, a growing list of examples points to destabilizing and denaturing properties, in particular for α-helical membrane proteins. Our comprehensive analysis stresses the importance of stringent controls when working with this class of detergents and when analyzing the structure and dynamics of membrane proteins in alkyl phosphocholine detergents.","lang":"eng"}],"day":"28","article_processing_charge":"No","date_created":"2020-09-18T10:05:35Z","volume":118,"keyword":["General Chemistry"],"title":"Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies","language":[{"iso":"eng"}],"publisher":"American Chemical Society","date_published":"2018-02-28T00:00:00Z","article_type":"original","month":"02","publication_status":"published","date_updated":"2021-01-12T08:19:18Z","extern":"1"},{"citation":{"chicago":"Aubret, Antoine, and Jérémie A Palacci. “Diffusiophoretic Design of Self-Spinning Microgears from Colloidal Microswimmers.” <i>Soft Matter</i>. Royal Society of Chemistry , 2018. <a href=\"https://doi.org/10.1039/c8sm01760c\">https://doi.org/10.1039/c8sm01760c</a>.","short":"A. Aubret, J.A. Palacci, Soft Matter 14 (2018) 9577–9588.","ista":"Aubret A, Palacci JA. 2018. Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. Soft Matter. 14(47), 9577–9588.","apa":"Aubret, A., &#38; Palacci, J. A. (2018). Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. <i>Soft Matter</i>. Royal Society of Chemistry . <a href=\"https://doi.org/10.1039/c8sm01760c\">https://doi.org/10.1039/c8sm01760c</a>","ama":"Aubret A, Palacci JA. Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. <i>Soft Matter</i>. 2018;14(47):9577-9588. doi:<a href=\"https://doi.org/10.1039/c8sm01760c\">10.1039/c8sm01760c</a>","mla":"Aubret, Antoine, and Jérémie A. Palacci. “Diffusiophoretic Design of Self-Spinning Microgears from Colloidal Microswimmers.” <i>Soft Matter</i>, vol. 14, no. 47, Royal Society of Chemistry , 2018, pp. 9577–88, doi:<a href=\"https://doi.org/10.1039/c8sm01760c\">10.1039/c8sm01760c</a>.","ieee":"A. Aubret and J. A. Palacci, “Diffusiophoretic design of self-spinning microgears from colloidal microswimmers,” <i>Soft Matter</i>, vol. 14, no. 47. Royal Society of Chemistry , pp. 9577–9588, 2018."},"external_id":{"arxiv":["1909.11121"],"pmid":["30456407"]},"arxiv":1,"intvolume":"        14","type":"journal_article","publication":"Soft Matter","doi":"10.1039/c8sm01760c","_id":"9053","quality_controlled":"1","page":"9577-9588","author":[{"first_name":"Antoine","full_name":"Aubret, Antoine","last_name":"Aubret"},{"orcid":"0000-0002-7253-9465","last_name":"Palacci","full_name":"Palacci, Jérémie A","first_name":"Jérémie A","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d"}],"pmid":1,"scopus_import":"1","extern":"1","abstract":[{"text":"The development of strategies to assemble microscopic machines from dissipative building blocks are essential on the route to novel active materials. We recently demonstrated the hierarchical self-assembly of phoretic microswimmers into self-spinning microgears and their synchronization by diffusiophoretic interactions [Aubret et al., Nat. Phys., 2018]. In this paper, we adopt a pedagogical approach and expose our strategy to control self-assembly and build machines using phoretic phenomena. We notably introduce Highly Inclined Laminated Optical sheets microscopy (HILO) to image and characterize anisotropic and dynamic diffusiophoretic interactions, which cannot be performed by conventional fluorescence microscopy. The dynamics of a (haematite) photocatalytic material immersed in (hydrogen peroxide) fuel under various illumination patterns is first described and quantitatively rationalized by a model of diffusiophoresis, the migration of a colloidal particle in a concentration gradient. It is further exploited to design phototactic microswimmers that direct towards the high intensity of light, as a result of the reorientation of the haematite in a light gradient. We finally show the assembly of self-spinning microgears from colloidal microswimmers and carefully characterize the interactions using HILO techniques. The results are compared with analytical and numerical predictions and agree quantitatively, stressing the important role played by concentration gradients induced by chemical activity to control and design interactions. Because the approach described hereby is generic, this works paves the way for the rational design of machines by controlling phoretic phenomena.","lang":"eng"}],"day":"21","date_created":"2021-02-01T13:44:41Z","title":"Diffusiophoretic design of self-spinning microgears from colloidal microswimmers","language":[{"iso":"eng"}],"main_file_link":[{"url":"https://arxiv.org/abs/1909.11121","open_access":"1"}],"volume":14,"keyword":["General Chemistry","Condensed Matter Physics"],"oa_version":"Preprint","publication_identifier":{"eissn":["1744-6848"],"issn":["1744-683X"]},"user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","issue":"47","year":"2018","status":"public","publisher":"Royal Society of Chemistry ","date_published":"2018-12-21T00:00:00Z","article_type":"original","month":"12","date_updated":"2023-02-23T13:47:43Z","publication_status":"published","article_processing_charge":"No","oa":1},{"publication_identifier":{"issn":["2041-1723"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Published Version","status":"public","year":"2017","month":"08","article_type":"original","date_published":"2017-08-30T00:00:00Z","date_updated":"2024-10-14T11:20:12Z","publication_status":"published","publisher":"Springer Nature","oa":1,"article_processing_charge":"No","article_number":"328","type":"journal_article","publication":"Nature Communications","citation":{"ista":"Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328.","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>.","short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (2017).","ieee":"A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","mla":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>, vol. 8, 328, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/s41467-017-00322-z\">10.1038/s41467-017-00322-z</a>.","apa":"Buchwalter, A., &#38; Hetzer, M. (2017). Nucleolar expansion and elevated protein translation in premature aging. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>","ama":"Buchwalter A, Hetzer M. Nucleolar expansion and elevated protein translation in premature aging. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/s41467-017-00322-z\">10.1038/s41467-017-00322-z</a>"},"external_id":{"pmid":["28855503"]},"intvolume":"         8","quality_controlled":"1","author":[{"last_name":"Buchwalter","first_name":"Abigail","full_name":"Buchwalter, Abigail"},{"orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"doi":"10.1038/s41467-017-00322-z","_id":"11065","extern":"1","scopus_import":"1","pmid":1,"title":"Nucleolar expansion and elevated protein translation in premature aging","language":[{"iso":"eng"}],"main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-00322-z","open_access":"1"}],"volume":8,"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"abstract":[{"lang":"eng","text":"Premature aging disorders provide an opportunity to study the mechanisms that drive aging. In Hutchinson-Gilford progeria syndrome (HGPS), a mutant form of the nuclear scaffold protein lamin A distorts nuclei and sequesters nuclear proteins. We sought to investigate protein homeostasis in this disease. Here, we report a widespread increase in protein turnover in HGPS-derived cells compared to normal cells. We determine that global protein synthesis is elevated as a consequence of activated nucleoli and enhanced ribosome biogenesis in HGPS-derived fibroblasts. Depleting normal lamin A or inducing mutant lamin A expression are each sufficient to drive nucleolar expansion. We further show that nucleolar size correlates with donor age in primary fibroblasts derived from healthy individuals and that ribosomal RNA production increases with age, indicating that nucleolar size and activity can serve as aging biomarkers. While limiting ribosome biogenesis extends lifespan in several systems, we show that increased ribosome biogenesis and activity are a hallmark of premature aging."}],"day":"30","date_created":"2022-04-07T07:45:50Z"},{"external_id":{"pmid":["29193964"]},"citation":{"ama":"Sawczyk M, Klajn R. Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. <i>Journal of the American Chemical Society</i>. 2017;139(49):17973-17978. doi:<a href=\"https://doi.org/10.1021/jacs.7b09111\">10.1021/jacs.7b09111</a>","apa":"Sawczyk, M., &#38; Klajn, R. (2017). Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jacs.7b09111\">https://doi.org/10.1021/jacs.7b09111</a>","mla":"Sawczyk, Michał, and Rafal Klajn. “Out-of-Equilibrium Aggregates and Coatings during Seeded Growth of Metallic Nanoparticles.” <i>Journal of the American Chemical Society</i>, vol. 139, no. 49, American Chemical Society, 2017, pp. 17973–78, doi:<a href=\"https://doi.org/10.1021/jacs.7b09111\">10.1021/jacs.7b09111</a>.","ieee":"M. Sawczyk and R. Klajn, “Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles,” <i>Journal of the American Chemical Society</i>, vol. 139, no. 49. American Chemical Society, pp. 17973–17978, 2017.","short":"M. Sawczyk, R. Klajn, Journal of the American Chemical Society 139 (2017) 17973–17978.","chicago":"Sawczyk, Michał, and Rafal Klajn. “Out-of-Equilibrium Aggregates and Coatings during Seeded Growth of Metallic Nanoparticles.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2017. <a href=\"https://doi.org/10.1021/jacs.7b09111\">https://doi.org/10.1021/jacs.7b09111</a>.","ista":"Sawczyk M, Klajn R. 2017. Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. Journal of the American Chemical Society. 139(49), 17973–17978."},"intvolume":"       139","publication":"Journal of the American Chemical Society","type":"journal_article","_id":"13380","doi":"10.1021/jacs.7b09111","quality_controlled":"1","page":"17973-17978","author":[{"full_name":"Sawczyk, Michał","first_name":"Michał","last_name":"Sawczyk"},{"last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal","first_name":"Rafal"}],"pmid":1,"extern":"1","scopus_import":"1","date_created":"2023-08-01T09:41:01Z","abstract":[{"text":"Although dissipative self-assembly is ubiquitous in nature, where it gives rise to structures and functions critical to life, examples of artificial systems featuring this mode of self-assembly are rare. Here, we identify the presence of ephemeral assemblies during seeded growth of gold nanoparticles. In this process, hydrazine reduces Au(III) ions, which attach to the existing nanoparticles “seeds”. The attachment is accompanied by a local increase in the concentration of a surfactant, which therefore forms a bilayer on nanoparticle surfaces, inducing their assembly. The resulting aggregates gradually disassemble as the surfactant concentration throughout the solution equilibrates. The lifetimes of the out-of-equilibrium aggregates depend on and can be controlled by the size of the constituent nanoparticles. We demonstrate the utility of our out-of-equilibrium aggregates to form transient reflective coatings on polar surfaces.","lang":"eng"}],"day":"01","language":[{"iso":"eng"}],"title":"Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"volume":139,"oa_version":"None","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2017","status":"public","issue":"49","publisher":"American Chemical Society","publication_status":"published","date_updated":"2024-10-14T12:15:25Z","date_published":"2017-12-01T00:00:00Z","month":"12","article_type":"original","article_processing_charge":"No"},{"type":"journal_article","publication":"Chemical Society Reviews","citation":{"apa":"van Esch, J. H., Klajn, R., &#38; Otto, S. (2017). Chemical systems out of equilibrium. <i>Chemical Society Reviews</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/c7cs90088k\">https://doi.org/10.1039/c7cs90088k</a>","ama":"van Esch JH, Klajn R, Otto S. Chemical systems out of equilibrium. <i>Chemical Society Reviews</i>. 2017;46(18):5474-5475. doi:<a href=\"https://doi.org/10.1039/c7cs90088k\">10.1039/c7cs90088k</a>","mla":"van Esch, Jan H., et al. “Chemical Systems out of Equilibrium.” <i>Chemical Society Reviews</i>, vol. 46, no. 18, Royal Society of Chemistry, 2017, pp. 5474–75, doi:<a href=\"https://doi.org/10.1039/c7cs90088k\">10.1039/c7cs90088k</a>.","ieee":"J. H. van Esch, R. Klajn, and S. Otto, “Chemical systems out of equilibrium,” <i>Chemical Society Reviews</i>, vol. 46, no. 18. Royal Society of Chemistry, pp. 5474–5475, 2017.","chicago":"Esch, Jan H. van, Rafal Klajn, and Sijbren Otto. “Chemical Systems out of Equilibrium.” <i>Chemical Society Reviews</i>. Royal Society of Chemistry, 2017. <a href=\"https://doi.org/10.1039/c7cs90088k\">https://doi.org/10.1039/c7cs90088k</a>.","short":"J.H. van Esch, R. Klajn, S. Otto, Chemical Society Reviews 46 (2017) 5474–5475.","ista":"van Esch JH, Klajn R, Otto S. 2017. Chemical systems out of equilibrium. Chemical Society Reviews. 46(18), 5474–5475."},"external_id":{"pmid":["28884760"]},"intvolume":"        46","quality_controlled":"1","page":"5474-5475","author":[{"last_name":"van Esch","first_name":"Jan H.","full_name":"van Esch, Jan H."},{"first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn"},{"full_name":"Otto, Sijbren","first_name":"Sijbren","last_name":"Otto"}],"doi":"10.1039/c7cs90088k","_id":"13382","scopus_import":"1","extern":"1","pmid":1,"title":"Chemical systems out of equilibrium","main_file_link":[{"url":"https://doi.org/10.1039/c7cs90088k","open_access":"1"}],"language":[{"iso":"eng"}],"volume":46,"keyword":["General Chemistry"],"day":"08","date_created":"2023-08-01T09:41:30Z","publication_identifier":{"eissn":["1460-4744"],"issn":["0306-0012"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Published Version","year":"2017","status":"public","issue":"18","date_published":"2017-09-08T00:00:00Z","month":"09","article_type":"letter_note","date_updated":"2024-10-14T12:15:48Z","publication_status":"published","publisher":"Royal Society of Chemistry","oa":1,"article_processing_charge":"No"},{"publisher":"Springer Nature","article_type":"original","month":"06","date_published":"2017-06-15T00:00:00Z","date_updated":"2023-08-22T08:26:06Z","publication_status":"published","article_processing_charge":"No","article_number":"15651","oa":1,"oa_version":"Published Version","publication_identifier":{"eissn":["2041-1723"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","year":"2017","pmid":1,"scopus_import":"1","extern":"1","abstract":[{"text":"Strong-field photoelectron holography and laser-induced electron diffraction (LIED) are two powerful emerging methods for probing the ultrafast dynamics of molecules. However, both of them have remained restricted to static systems and to nuclear dynamics induced by strong-field ionization. Here we extend these promising methods to image purely electronic valence-shell dynamics in molecules using photoelectron holography. In the same experiment, we use LIED and photoelectron holography simultaneously, to observe coupled electronic-rotational dynamics taking place on similar timescales. These results offer perspectives for imaging ultrafast dynamics of molecules on femtosecond to attosecond timescales.","lang":"eng"}],"day":"15","date_created":"2023-08-10T06:36:09Z","title":"Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering","main_file_link":[{"url":"https://doi.org/10.1038/ncomms15651","open_access":"1"}],"language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"volume":8,"citation":{"mla":"Walt, Samuel G., et al. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” <i>Nature Communications</i>, vol. 8, 15651, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>.","ieee":"S. G. Walt <i>et al.</i>, “Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","ama":"Walt SG, Bhargava Ram N, Atala M, et al. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>","apa":"Walt, S. G., Bhargava Ram, N., Atala, M., Shvetsov-Shilovski, N. I., von Conta, A., Baykusheva, D. R., … Wörner, H. J. (2017). Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms15651\">https://doi.org/10.1038/ncomms15651</a>","ista":"Walt SG, Bhargava Ram N, Atala M, Shvetsov-Shilovski NI, von Conta A, Baykusheva DR, Lein M, Wörner HJ. 2017. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. Nature Communications. 8, 15651.","short":"S.G. Walt, N. Bhargava Ram, M. Atala, N.I. Shvetsov-Shilovski, A. von Conta, D.R. Baykusheva, M. Lein, H.J. Wörner, Nature Communications 8 (2017).","chicago":"Walt, Samuel G., Niraghatam Bhargava Ram, Marcos Atala, Nikolay I Shvetsov-Shilovski, Aaron von Conta, Denitsa Rangelova Baykusheva, Manfred Lein, and Hans Jakob Wörner. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/ncomms15651\">https://doi.org/10.1038/ncomms15651</a>."},"external_id":{"pmid":["28643771"]},"intvolume":"         8","type":"journal_article","publication":"Nature Communications","doi":"10.1038/ncomms15651","_id":"14005","quality_controlled":"1","author":[{"last_name":"Walt","first_name":"Samuel G.","full_name":"Walt, Samuel G."},{"first_name":"Niraghatam","full_name":"Bhargava Ram, Niraghatam","last_name":"Bhargava Ram"},{"first_name":"Marcos","full_name":"Atala, Marcos","last_name":"Atala"},{"last_name":"Shvetsov-Shilovski","first_name":"Nikolay I","full_name":"Shvetsov-Shilovski, Nikolay I"},{"first_name":"Aaron","full_name":"von Conta, Aaron","last_name":"von Conta"},{"last_name":"Baykusheva","first_name":"Denitsa Rangelova","full_name":"Baykusheva, Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530"},{"first_name":"Manfred","full_name":"Lein, Manfred","last_name":"Lein"},{"full_name":"Wörner, Hans Jakob","first_name":"Hans Jakob","last_name":"Wörner"}]},{"has_accepted_license":"1","status":"public","year":"2017","issue":"12","oa_version":"Published Version","file":[{"date_updated":"2021-11-29T09:00:40Z","success":1,"creator":"cchlebak","checksum":"1cf3e5e5342f2d728f47560acc3ec560","access_level":"open_access","file_size":2635263,"content_type":"application/pdf","file_id":"10371","relation":"main_file","file_name":"2017_ACSCentSci_Simunovic.pdf","date_created":"2021-11-29T09:00:40Z"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"publication_identifier":{"eissn":["2374-7951"],"issn":["2374-7943"]},"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","article_processing_charge":"No","oa":1,"publisher":"American Chemical Society","publication_status":"published","date_updated":"2021-11-29T09:28:06Z","article_type":"original","date_published":"2017-11-21T00:00:00Z","month":"11","_id":"10369","doi":"10.1021/acscentsci.7b00392","quality_controlled":"1","page":"1246-1253","author":[{"full_name":"Simunovic, Mijo","first_name":"Mijo","last_name":"Simunovic"},{"orcid":"0000-0002-7854-2139","last_name":"Šarić","first_name":"Anđela","full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b"},{"last_name":"Henderson","full_name":"Henderson, J. Michael","first_name":"J. Michael"},{"last_name":"Lee","first_name":"Ka Yee C.","full_name":"Lee, Ka Yee C."},{"last_name":"Voth","full_name":"Voth, Gregory A.","first_name":"Gregory A."}],"external_id":{"pmid":["29296664"]},"ddc":["540"],"acknowledgement":"M.S. and G.A.V. acknowledge their research reported in this publication as being supported by the National Institute of General Medical Sciences of the National Institutes of Health under Award Number R01-GM063796. Computational resources were provided to M.S. and G.A.V. by the National Science Foundation through XSEDE (Grant TG-MCA94P017, supercomputers Stampede and Gordon), and also by the Blue Waters computing project at the National Center for Supercomputing Applications (University of Illinois at Urbana–Champaign, NSF Awards OCI-0725070 and ACI-1238993). A.Š. acknowledges support from the Human Frontier Science Program and Royal Society. J.M.H. and K.Y.C.L. acknowledge the support from the National Science Foundation (Grant MCB-1413613) and the NSF-supported MRSEC program at the University of Chicago (Grant DMR-1420709). We are grateful to Carsten Mim and Vinzenz Unger of Northwestern University for generously providing us with the protein. We thank all the members of the Voth group for fruitful discussions, especially John M. A. Grime.","citation":{"mla":"Simunovic, Mijo, et al. “Long-Range Organization of Membrane-Curving Proteins.” <i>ACS Central Science</i>, vol. 3, no. 12, American Chemical Society, 2017, pp. 1246–53, doi:<a href=\"https://doi.org/10.1021/acscentsci.7b00392\">10.1021/acscentsci.7b00392</a>.","ieee":"M. Simunovic, A. Šarić, J. M. Henderson, K. Y. C. Lee, and G. A. Voth, “Long-range organization of membrane-curving proteins,” <i>ACS Central Science</i>, vol. 3, no. 12. American Chemical Society, pp. 1246–1253, 2017.","apa":"Simunovic, M., Šarić, A., Henderson, J. M., Lee, K. Y. C., &#38; Voth, G. A. (2017). Long-range organization of membrane-curving proteins. <i>ACS Central Science</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acscentsci.7b00392\">https://doi.org/10.1021/acscentsci.7b00392</a>","ama":"Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. Long-range organization of membrane-curving proteins. <i>ACS Central Science</i>. 2017;3(12):1246-1253. doi:<a href=\"https://doi.org/10.1021/acscentsci.7b00392\">10.1021/acscentsci.7b00392</a>","ista":"Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. 2017. Long-range organization of membrane-curving proteins. ACS Central Science. 3(12), 1246–1253.","chicago":"Simunovic, Mijo, Anđela Šarić, J. Michael Henderson, Ka Yee C. Lee, and Gregory A. Voth. “Long-Range Organization of Membrane-Curving Proteins.” <i>ACS Central Science</i>. American Chemical Society, 2017. <a href=\"https://doi.org/10.1021/acscentsci.7b00392\">https://doi.org/10.1021/acscentsci.7b00392</a>.","short":"M. Simunovic, A. Šarić, J.M. Henderson, K.Y.C. Lee, G.A. Voth, ACS Central Science 3 (2017) 1246–1253."},"intvolume":"         3","publication":"ACS Central Science","type":"journal_article","date_created":"2021-11-29T08:49:50Z","abstract":[{"text":"Biological membranes have a central role in mediating the organization of membrane-curving proteins, a dynamic process that has proven to be challenging to probe experimentally. Using atomic force microscopy, we capture the hierarchically organized assemblies of Bin/amphiphysin/Rvs (BAR) proteins on supported lipid membranes. Their structure reveals distinct long linear aggregates of proteins, regularly spaced by up to 300 nm. Employing accurate free-energy calculations from large-scale coarse-grained computer simulations, we found that the membrane mediates the interaction among protein filaments as a combination of short- and long-ranged interactions. The long-ranged component acts at strikingly long distances, giving rise to a variety of micron-sized ordered patterns. This mechanism may contribute to the long-ranged spatiotemporal control of membrane remodeling by proteins in the cell.","lang":"eng"}],"day":"21","language":[{"iso":"eng"}],"main_file_link":[{"open_access":"1","url":"https://pubs.acs.org/doi/10.1021/acscentsci.7b00392"}],"title":"Long-range organization of membrane-curving proteins","volume":3,"keyword":["general chemical engineering","general chemistry"],"file_date_updated":"2021-11-29T09:00:40Z","pmid":1,"scopus_import":"1","extern":"1"},{"oa":1,"article_processing_charge":"No","article_type":"original","month":"08","date_published":"2017-08-31T00:00:00Z","publication_status":"published","date_updated":"2021-11-29T10:00:00Z","publisher":"Royal Society of Chemistry","status":"public","issue":"10","year":"2017","publication_identifier":{"eissn":["2041-6539"],"issn":["2041-6520"]},"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","oa_version":"Published Version","tmp":{"image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)","short":"CC BY-NC (3.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/3.0/legalcode"},"title":"Scaling behaviour and rate-determining steps in filamentous self-assembly","license":"https://creativecommons.org/licenses/by-nc/3.0/","main_file_link":[{"open_access":"1","url":"https://pubs.rsc.org/en/content/articlelanding/2017/SC/C7SC01965C"}],"language":[{"iso":"eng"}],"keyword":["general chemistry"],"volume":8,"abstract":[{"text":"The formation of filaments from naturally occurring protein molecules is a process at the core of a range of functional and aberrant biological phenomena, such as the assembly of the cytoskeleton or the appearance of aggregates in Alzheimer's disease. The macroscopic behaviour associated with such processes is remarkably diverse, ranging from simple nucleated growth to highly cooperative processes with a well-defined lagtime. Thus, conventionally, different molecular mechanisms have been used to explain the self-assembly of different proteins. Here we show that this range of behaviour can be quantitatively captured by a single unifying Petri net that describes filamentous growth in terms of aggregate number and aggregate mass concentrations. By considering general features associated with a particular network connectivity, we are able to establish directly the rate-determining steps of the overall aggregation reaction from the system's scaling behaviour. We illustrate the power of this framework on a range of different experimental and simulated aggregating systems. The approach is general and will be applicable to any future extensions of the reaction network of filamentous self-assembly.","lang":"eng"}],"day":"31","date_created":"2021-11-29T09:29:31Z","scopus_import":"1","extern":"1","pmid":1,"quality_controlled":"1","author":[{"last_name":"Meisl","full_name":"Meisl, Georg","first_name":"Georg"},{"last_name":"Rajah","full_name":"Rajah, Luke","first_name":"Luke"},{"full_name":"Cohen, Samuel A. I.","first_name":"Samuel A. I.","last_name":"Cohen"},{"last_name":"Pfammatter","full_name":"Pfammatter, Manuela","first_name":"Manuela"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","full_name":"Šarić, Anđela","first_name":"Anđela","last_name":"Šarić","orcid":"0000-0002-7854-2139"},{"last_name":"Hellstrand","first_name":"Erik","full_name":"Hellstrand, Erik"},{"last_name":"Buell","full_name":"Buell, Alexander K.","first_name":"Alexander K."},{"last_name":"Aguzzi","full_name":"Aguzzi, Adriano","first_name":"Adriano"},{"last_name":"Linse","first_name":"Sara","full_name":"Linse, Sara"},{"full_name":"Vendruscolo, Michele","first_name":"Michele","last_name":"Vendruscolo"},{"full_name":"Dobson, Christopher M.","first_name":"Christopher M.","last_name":"Dobson"},{"full_name":"Knowles, Tuomas P. J.","first_name":"Tuomas P. J.","last_name":"Knowles"}],"page":"7087-7097","doi":"10.1039/c7sc01965c","_id":"10374","publication":"Chemical Science","type":"journal_article","citation":{"ama":"Meisl G, Rajah L, Cohen SAI, et al. Scaling behaviour and rate-determining steps in filamentous self-assembly. <i>Chemical Science</i>. 2017;8(10):7087-7097. doi:<a href=\"https://doi.org/10.1039/c7sc01965c\">10.1039/c7sc01965c</a>","apa":"Meisl, G., Rajah, L., Cohen, S. A. I., Pfammatter, M., Šarić, A., Hellstrand, E., … Knowles, T. P. J. (2017). Scaling behaviour and rate-determining steps in filamentous self-assembly. <i>Chemical Science</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/c7sc01965c\">https://doi.org/10.1039/c7sc01965c</a>","mla":"Meisl, Georg, et al. “Scaling Behaviour and Rate-Determining Steps in Filamentous Self-Assembly.” <i>Chemical Science</i>, vol. 8, no. 10, Royal Society of Chemistry, 2017, pp. 7087–97, doi:<a href=\"https://doi.org/10.1039/c7sc01965c\">10.1039/c7sc01965c</a>.","ieee":"G. Meisl <i>et al.</i>, “Scaling behaviour and rate-determining steps in filamentous self-assembly,” <i>Chemical Science</i>, vol. 8, no. 10. Royal Society of Chemistry, pp. 7087–7097, 2017.","short":"G. Meisl, L. Rajah, S.A.I. Cohen, M. Pfammatter, A. Šarić, E. Hellstrand, A.K. Buell, A. Aguzzi, S. Linse, M. Vendruscolo, C.M. Dobson, T.P.J. Knowles, Chemical Science 8 (2017) 7087–7097.","chicago":"Meisl, Georg, Luke Rajah, Samuel A. I. Cohen, Manuela Pfammatter, Anđela Šarić, Erik Hellstrand, Alexander K. Buell, et al. “Scaling Behaviour and Rate-Determining Steps in Filamentous Self-Assembly.” <i>Chemical Science</i>. Royal Society of Chemistry, 2017. <a href=\"https://doi.org/10.1039/c7sc01965c\">https://doi.org/10.1039/c7sc01965c</a>.","ista":"Meisl G, Rajah L, Cohen SAI, Pfammatter M, Šarić A, Hellstrand E, Buell AK, Aguzzi A, Linse S, Vendruscolo M, Dobson CM, Knowles TPJ. 2017. Scaling behaviour and rate-determining steps in filamentous self-assembly. Chemical Science. 8(10), 7087–7097."},"acknowledgement":"The research leading to these results has received funding from the European Research Council under the European Union's Seventh Framework Programme (FP7/2007-2013) through the ERC grant PhysProt (agreement no. 337969) (SL, TPJK), Sidney Sussex College Cambridge (GM), the Frances and Augusta Newman Foundation (TPJK), the Biotechnology and Biological Science Research Council (TPJK), the Swedish Research Council (SL), the Academy of Medical Sciences (AŠ), Wellcome Trust (AŠ), and the Cambridge Centre for Misfolding Diseases (CMD, TPJK, MV).","ddc":["540"],"external_id":{"pmid":["29147538"]},"intvolume":"         8"},{"status":"public","issue":"28","year":"2017","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/3.0/legalcode","short":"CC BY (3.0)","name":"Creative Commons Attribution 3.0 Unported (CC BY 3.0)","image":"/images/cc_by.png"},"oa_version":"Published Version","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","publication_identifier":{"issn":["1744-683X"],"eissn":["1744-6848"]},"article_processing_charge":"No","oa":1,"publisher":"Royal Society of Chemistry","publication_status":"published","date_updated":"2021-11-29T10:33:36Z","date_published":"2017-06-15T00:00:00Z","article_type":"original","month":"06","_id":"10375","doi":"10.1039/c7sm00433h","page":"4924-4930","author":[{"last_name":"Vahid","full_name":"Vahid, Afshin","first_name":"Afshin"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","full_name":"Šarić, Anđela","first_name":"Anđela","last_name":"Šarić","orcid":"0000-0002-7854-2139"},{"full_name":"Idema, Timon","first_name":"Timon","last_name":"Idema"}],"quality_controlled":"1","intvolume":"        13","arxiv":1,"external_id":{"arxiv":["1703.00776"],"pmid":["28677712"]},"citation":{"ista":"Vahid A, Šarić A, Idema T. 2017. Curvature variation controls particle aggregation on fluid vesicles. Soft Matter. 13(28), 4924–4930.","chicago":"Vahid, Afshin, Anđela Šarić, and Timon Idema. “Curvature Variation Controls Particle Aggregation on Fluid Vesicles.” <i>Soft Matter</i>. Royal Society of Chemistry, 2017. <a href=\"https://doi.org/10.1039/c7sm00433h\">https://doi.org/10.1039/c7sm00433h</a>.","short":"A. Vahid, A. Šarić, T. Idema, Soft Matter 13 (2017) 4924–4930.","mla":"Vahid, Afshin, et al. “Curvature Variation Controls Particle Aggregation on Fluid Vesicles.” <i>Soft Matter</i>, vol. 13, no. 28, Royal Society of Chemistry, 2017, pp. 4924–30, doi:<a href=\"https://doi.org/10.1039/c7sm00433h\">10.1039/c7sm00433h</a>.","ieee":"A. Vahid, A. Šarić, and T. Idema, “Curvature variation controls particle aggregation on fluid vesicles,” <i>Soft Matter</i>, vol. 13, no. 28. Royal Society of Chemistry, pp. 4924–4930, 2017.","apa":"Vahid, A., Šarić, A., &#38; Idema, T. (2017). Curvature variation controls particle aggregation on fluid vesicles. <i>Soft Matter</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/c7sm00433h\">https://doi.org/10.1039/c7sm00433h</a>","ama":"Vahid A, Šarić A, Idema T. Curvature variation controls particle aggregation on fluid vesicles. <i>Soft Matter</i>. 2017;13(28):4924-4930. doi:<a href=\"https://doi.org/10.1039/c7sm00433h\">10.1039/c7sm00433h</a>"},"acknowledgement":"This work was supported by the Netherlands Organisation for Scientific Research (NWO/OCW), as part of the Frontiers of Nanoscience program.","publication":"Soft Matter","type":"journal_article","date_created":"2021-11-29T10:00:39Z","day":"15","abstract":[{"lang":"eng","text":"Cellular membranes exhibit a large variety of shapes, strongly coupled to their function. Many biological processes involve dynamic reshaping of membranes, usually mediated by proteins. This interaction works both ways: while proteins influence the membrane shape, the membrane shape affects the interactions between the proteins. To study these membrane-mediated interactions on closed and anisotropically curved membranes, we use colloids adhered to ellipsoidal membrane vesicles as a model system. We find that two particles on a closed system always attract each other, and tend to align with the direction of largest curvature. Multiple particles form arcs, or, at large enough numbers, a complete ring surrounding the vesicle in its equatorial plane. The resulting vesicle shape resembles a snowman. Our results indicate that these physical interactions on membranes with anisotropic shapes can be exploited by cells to drive macromolecules to preferred regions of cellular or intracellular membranes, and utilized to initiate dynamic processes such as cell division. The same principle could be used to find the midplane of an artificial vesicle, as a first step towards dividing it into two equal parts."}],"volume":13,"keyword":["condensed matter physics","general chemistry"],"language":[{"iso":"eng"}],"main_file_link":[{"open_access":"1","url":"https://pubs.rsc.org/en/content/articlelanding/2017/SM/C7SM00433H"}],"title":"Curvature variation controls particle aggregation on fluid vesicles","pmid":1,"scopus_import":"1","extern":"1"},{"year":"2017","author":[{"first_name":"Diego F.","full_name":"Gauto, Diego F.","last_name":"Gauto"},{"full_name":"Hessel, Audrey","first_name":"Audrey","last_name":"Hessel"},{"last_name":"Rovó","first_name":"Petra","full_name":"Rovó, Petra"},{"last_name":"Kurauskas","full_name":"Kurauskas, Vilius","first_name":"Vilius"},{"first_name":"Rasmus","full_name":"Linser, Rasmus","last_name":"Linser"},{"full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda"}],"status":"public","issue":"10","page":"86-95","quality_controlled":"1","doi":"10.1016/j.ssnmr.2017.04.002","_id":"8447","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","type":"journal_article","publication":"Solid State Nuclear Magnetic Resonance","publication_identifier":{"issn":["0926-2040"]},"intvolume":"        87","citation":{"short":"D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid State Nuclear Magnetic Resonance 87 (2017) 86–95.","chicago":"Gauto, Diego F., Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser, and Paul Schanda. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” <i>Solid State Nuclear Magnetic Resonance</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>.","ista":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. 2017. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 87(10), 86–95.","ama":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State Nuclear Magnetic Resonance</i>. 2017;87(10):86-95. doi:<a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">10.1016/j.ssnmr.2017.04.002</a>","apa":"Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., &#38; Schanda, P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State Nuclear Magnetic Resonance</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>","ieee":"D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda, “Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals,” <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.","mla":"Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10, Elsevier, 2017, pp. 86–95, doi:<a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">10.1016/j.ssnmr.2017.04.002</a>."},"oa_version":"None","keyword":["Nuclear and High Energy Physics","Instrumentation","General Chemistry","Radiation"],"volume":87,"title":"Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals","language":[{"iso":"eng"}],"article_processing_charge":"No","day":"01","abstract":[{"lang":"eng","text":"Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region that undergoes microsecond motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation dispersion, to probe how the G53A mutation alters these dynamics. We report a population-inversion of conformational states: the conformation that in the wild-type protein is populated only sparsely becomes the predominant state. We furthermore explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics. We show that while quantitative interpretation of 1H relaxation remains beyond reach under the experimental conditions, due to coherent contributions to decay, one may extract qualitative information about flexibility."}],"date_created":"2020-09-18T10:06:18Z","month":"10","article_type":"original","date_published":"2017-10-01T00:00:00Z","publication_status":"published","date_updated":"2021-01-12T08:19:20Z","extern":"1","publisher":"Elsevier"}]