[{"page":"858-869","article_type":"original","citation":{"mla":"Rovó, Petra, et al. “Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.” Journal of the American Chemical Society, vol. 141, no. 2, American Chemical Society, 2019, pp. 858–69, doi:10.1021/jacs.8b09258.","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.” Journal of the American Chemical Society. American Chemical Society, 2019. https://doi.org/10.1021/jacs.8b09258.","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. Journal of the American Chemical Society. 2019;141(2):858-869. doi:10.1021/jacs.8b09258","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.","apa":"Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., 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. American Chemical Society. https://doi.org/10.1021/jacs.8b09258","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,” Journal of the American Chemical Society, vol. 141, no. 2. American Chemical Society, pp. 858–869, 2019."},"publication":"Journal of the American Chemical Society","date_published":"2019-01-08T00:00:00Z","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"article_processing_charge":"No","day":"08","intvolume":" 141","status":"public","title":"Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques","_id":"8413","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Submitted Version","type":"journal_article","issue":"2","abstract":[{"lang":"eng","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."}],"quality_controlled":"1","external_id":{"pmid":["30620186"]},"language":[{"iso":"eng"}],"doi":"10.1021/jacs.8b09258","publication_identifier":{"issn":["0002-7863","1520-5126"]},"month":"01","publisher":"American Chemical Society","publication_status":"published","pmid":1,"year":"2019","volume":141,"date_updated":"2021-01-12T08:19:07Z","date_created":"2020-09-17T10:29:50Z","author":[{"full_name":"Rovó, Petra","last_name":"Rovó","first_name":"Petra"},{"full_name":"Smith, Colin A.","first_name":"Colin A.","last_name":"Smith"},{"last_name":"Gauto","first_name":"Diego","full_name":"Gauto, Diego"},{"full_name":"de Groot, Bert L.","last_name":"de Groot","first_name":"Bert L."},{"full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"},{"full_name":"Linser, Rasmus","first_name":"Rasmus","last_name":"Linser"}],"extern":"1"},{"extern":"1","author":[{"first_name":"Diego F.","last_name":"Gauto","full_name":"Gauto, Diego F."},{"first_name":"Pavel","last_name":"Macek","full_name":"Macek, Pavel"},{"full_name":"Barducci, Alessandro","last_name":"Barducci","first_name":"Alessandro"},{"first_name":"Hugo","last_name":"Fraga","full_name":"Fraga, Hugo"},{"full_name":"Hessel, Audrey","first_name":"Audrey","last_name":"Hessel"},{"first_name":"Tsutomu","last_name":"Terauchi","full_name":"Terauchi, Tsutomu"},{"full_name":"Gajan, David","first_name":"David","last_name":"Gajan"},{"full_name":"Miyanoiri, Yohei","last_name":"Miyanoiri","first_name":"Yohei"},{"full_name":"Boisbouvier, Jerome","last_name":"Boisbouvier","first_name":"Jerome"},{"last_name":"Lichtenecker","first_name":"Roman","full_name":"Lichtenecker, Roman"},{"full_name":"Kainosho, Masatsune","first_name":"Masatsune","last_name":"Kainosho"},{"last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"}],"date_created":"2020-09-17T10:29:00Z","date_updated":"2021-01-12T08:19:04Z","volume":141,"year":"2019","pmid":1,"publication_status":"published","publisher":"American Chemical Society","month":"06","publication_identifier":{"issn":["0002-7863","1520-5126"]},"doi":"10.1021/jacs.9b04219","language":[{"iso":"eng"}],"external_id":{"pmid":["31199882"]},"quality_controlled":"1","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"}],"issue":"28","type":"journal_article","oa_version":"Submitted Version","_id":"8408","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","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","intvolume":" 141","day":"14","article_processing_charge":"No","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"date_published":"2019-06-14T00:00:00Z","publication":"Journal of the American Chemical Society","citation":{"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.” Journal of the American Chemical Society, vol. 141, no. 28, American Chemical Society, 2019, pp. 11183–95, doi:10.1021/jacs.9b04219.","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.” Journal of the American Chemical Society. American Chemical Society, 2019. https://doi.org/10.1021/jacs.9b04219.","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. Journal of the American Chemical Society. 2019;141(28):11183-11195. doi:10.1021/jacs.9b04219","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.","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. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.9b04219","ieee":"D. F. Gauto 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,” Journal of the American Chemical Society, vol. 141, no. 28. American Chemical Society, pp. 11183–11195, 2019."},"article_type":"original","page":"11183-11195"},{"volume":136,"oa_version":"None","date_updated":"2021-01-12T08:19:24Z","date_created":"2020-09-18T10:07:52Z","author":[{"last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"},{"full_name":"Triboulet, Sébastien","first_name":"Sébastien","last_name":"Triboulet"},{"full_name":"Laguri, Cédric","last_name":"Laguri","first_name":"Cédric"},{"full_name":"Bougault, Catherine M.","last_name":"Bougault","first_name":"Catherine M."},{"full_name":"Ayala, Isabel","last_name":"Ayala","first_name":"Isabel"},{"full_name":"Callon, Morgane","last_name":"Callon","first_name":"Morgane"},{"last_name":"Arthur","first_name":"Michel","full_name":"Arthur, Michel"},{"full_name":"Simorre, Jean-Pierre","first_name":"Jean-Pierre","last_name":"Simorre"}],"publisher":"American Chemical Society","intvolume":" 136","title":"Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan","publication_status":"published","status":"public","_id":"8458","year":"2014","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","issue":"51","abstract":[{"lang":"eng","text":"The maintenance of bacterial cell shape and integrity is largely attributed to peptidoglycan, a highly cross-linked biopolymer. The transpeptidases that perform this cross-linking are important targets for antibiotics. Despite this biomedical importance, to date no structure of a protein in complex with an intact bacterial peptidoglycan has been resolved, primarily due to the large size and flexibility of peptidoglycan sacculi. Here we use solid-state NMR spectroscopy to derive for the first time an atomic model of an l,d-transpeptidase from Bacillus subtilis bound to its natural substrate, the intact B. subtilis peptidoglycan. Importantly, the model obtained from protein chemical shift perturbation data shows that both domains—the catalytic domain as well as the proposed peptidoglycan recognition domain—are important for the interaction and reveals a novel binding motif that involves residues outside of the classical enzymatic pocket. Experiments on mutants and truncated protein constructs independently confirm the binding site and the implication of both domains. Through measurements of dipolar-coupling derived order parameters of bond motion we show that protein binding reduces the flexibility of peptidoglycan. This first report of an atomic model of a protein–peptidoglycan complex paves the way for the design of new antibiotic drugs targeting l,d-transpeptidases. The strategy developed here can be extended to the study of a large variety of enzymes involved in peptidoglycan morphogenesis."}],"type":"journal_article","language":[{"iso":"eng"}],"date_published":"2014-11-27T00:00:00Z","doi":"10.1021/ja5105987","page":"17852-17860","quality_controlled":"1","article_type":"original","citation":{"chicago":"Schanda, Paul, Sébastien Triboulet, Cédric Laguri, Catherine M. Bougault, Isabel Ayala, Morgane Callon, Michel Arthur, and Jean-Pierre Simorre. “Atomic Model of a Cell-Wall Cross-Linking Enzyme in Complex with an Intact Bacterial Peptidoglycan.” Journal of the American Chemical Society. American Chemical Society, 2014. https://doi.org/10.1021/ja5105987.","mla":"Schanda, Paul, et al. “Atomic Model of a Cell-Wall Cross-Linking Enzyme in Complex with an Intact Bacterial Peptidoglycan.” Journal of the American Chemical Society, vol. 136, no. 51, American Chemical Society, 2014, pp. 17852–60, doi:10.1021/ja5105987.","short":"P. Schanda, S. Triboulet, C. Laguri, C.M. Bougault, I. Ayala, M. Callon, M. Arthur, J.-P. Simorre, Journal of the American Chemical Society 136 (2014) 17852–17860.","ista":"Schanda P, Triboulet S, Laguri C, Bougault CM, Ayala I, Callon M, Arthur M, Simorre J-P. 2014. Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan. Journal of the American Chemical Society. 136(51), 17852–17860.","ieee":"P. Schanda et al., “Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan,” Journal of the American Chemical Society, vol. 136, no. 51. American Chemical Society, pp. 17852–17860, 2014.","apa":"Schanda, P., Triboulet, S., Laguri, C., Bougault, C. M., Ayala, I., Callon, M., … Simorre, J.-P. (2014). Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja5105987","ama":"Schanda P, Triboulet S, Laguri C, et al. Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan. Journal of the American Chemical Society. 2014;136(51):17852-17860. doi:10.1021/ja5105987"},"publication":"Journal of the American Chemical Society","publication_identifier":{"issn":["0002-7863","1520-5126"]},"article_processing_charge":"No","month":"11","day":"27"},{"publication":"Journal of the American Chemical Society","citation":{"ama":"Ottakam Thotiyl MM, Freunberger SA, Peng Z, Bruce PG. The carbon electrode in nonaqueous Li–O2 cells. Journal of the American Chemical Society. 2012;135(1):494-500. doi:10.1021/ja310258x","apa":"Ottakam Thotiyl, M. M., Freunberger, S. A., Peng, Z., & Bruce, P. G. (2012). The carbon electrode in nonaqueous Li–O2 cells. Journal of the American Chemical Society. ACS. https://doi.org/10.1021/ja310258x","ieee":"M. M. Ottakam Thotiyl, S. A. Freunberger, Z. Peng, and P. G. Bruce, “The carbon electrode in nonaqueous Li–O2 cells,” Journal of the American Chemical Society, vol. 135, no. 1. ACS, pp. 494–500, 2012.","ista":"Ottakam Thotiyl MM, Freunberger SA, Peng Z, Bruce PG. 2012. The carbon electrode in nonaqueous Li–O2 cells. Journal of the American Chemical Society. 135(1), 494–500.","short":"M.M. Ottakam Thotiyl, S.A. Freunberger, Z. Peng, P.G. Bruce, Journal of the American Chemical Society 135 (2012) 494–500.","mla":"Ottakam Thotiyl, Muhammed M., et al. “The Carbon Electrode in Nonaqueous Li–O2 Cells.” Journal of the American Chemical Society, vol. 135, no. 1, ACS, 2012, pp. 494–500, doi:10.1021/ja310258x.","chicago":"Ottakam Thotiyl, Muhammed M., Stefan Alexander Freunberger, Zhangquan Peng, and Peter G. Bruce. “The Carbon Electrode in Nonaqueous Li–O2 Cells.” Journal of the American Chemical Society. ACS, 2012. https://doi.org/10.1021/ja310258x."},"quality_controlled":"1","article_type":"original","page":"494-500","doi":"10.1021/ja310258x","date_published":"2012-11-28T00:00:00Z","language":[{"iso":"eng"}],"day":"28","month":"11","article_processing_charge":"No","publication_identifier":{"issn":["0002-7863","1520-5126"]},"year":"2012","_id":"7308","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"The carbon electrode in nonaqueous Li–O2 cells","publication_status":"published","status":"public","intvolume":" 135","publisher":"ACS","author":[{"last_name":"Ottakam Thotiyl","first_name":"Muhammed M.","full_name":"Ottakam Thotiyl, Muhammed M."},{"orcid":"0000-0003-2902-5319","id":"A8CA28E6-CE23-11E9-AD2D-EC27E6697425","last_name":"Freunberger","first_name":"Stefan Alexander","full_name":"Freunberger, Stefan Alexander"},{"last_name":"Peng","first_name":"Zhangquan","full_name":"Peng, Zhangquan"},{"full_name":"Bruce, Peter G.","last_name":"Bruce","first_name":"Peter G."}],"date_updated":"2021-01-12T08:12:56Z","date_created":"2020-01-15T12:18:57Z","oa_version":"None","volume":135,"type":"journal_article","abstract":[{"text":"Carbon has been used widely as the basis of porous cathodes for nonaqueous Li–O2 cells. However, the stability of carbon and the effect of carbon on electrolyte decomposition in such cells are complex and depend on the hydrophobicity/hydrophilicity of the carbon surface. Analyzing carbon cathodes, cycled in Li–O2 cells between 2 and 4 V, using acid treatment and Fenton’s reagent, and combined with differential electrochemical mass spectrometry and FTIR, demonstrates the following: Carbon is relatively stable below 3.5 V (vs Li/Li+) on discharge or charge, especially so for hydrophobic carbon, but is unstable on charging above 3.5 V (in the presence of Li2O2), oxidatively decomposing to form Li2CO3. Direct chemical reaction with Li2O2 accounts for only a small proportion of the total carbon decomposition on cycling. Carbon promotes electrolyte decomposition during discharge and charge in a Li–O2 cell, giving rise to Li2CO3 and Li carboxylates (DMSO and tetraglyme electrolytes). The Li2CO3 and Li carboxylates present at the end of discharge and those that form on charge result in polarization on the subsequent charge. Li2CO3 (derived from carbon and from the electrolyte) as well as the Li carboxylates (derived from the electrolyte) decompose and form on charging. Oxidation of Li2CO3 on charging to ∼4 V is incomplete; Li2CO3 accumulates on cycling resulting in electrode passivation and capacity fading. Hydrophilic carbon is less stable and more catalytically active toward electrolyte decomposition than carbon with a hydrophobic surface. If the Li–O2 cell could be charged at or below 3.5 V, then carbon may be relatively stable, however, its ability to promote electrolyte decomposition, presenting problems for its use in a practical Li–O2 battery. The results emphasize that stable cycling of Li2O2 at the cathode in a Li–O2 cell depends on the synergy between electrolyte and electrode; the stability of the electrode and the electrolyte cannot be considered in isolation.","lang":"eng"}],"issue":"1","extern":"1"},{"extern":"1","issue":"18","abstract":[{"lang":"eng","text":"Stability of the electrolyte toward reduced oxygen species generated at the cathode is a crucial challenge for the rechargeable nonaqueous Li–O2 battery. Here, we investigate dimethylformamide as the basis of an electrolyte. Although reactions at the O2 cathode on the first discharge–charge cycle are dominated by reversible Li2O2 formation/decomposition, there is also electrolyte decomposition, which increases on cycling. The products of decomposition at the cathode on discharge are Li2O2, Li2CO3, HCO2Li, CH3CO2Li, NO, H2O, and CO2. Li2CO3 accumulates in the electrode with cycling. The stability of dimethylformamide toward reduced oxygen species is insufficient for its use in the rechargeable nonaqueous Li–O2 battery."}],"type":"journal_article","volume":134,"oa_version":"None","date_updated":"2021-01-12T08:12:58Z","date_created":"2020-01-15T12:19:36Z","author":[{"full_name":"Chen, Yuhui","last_name":"Chen","first_name":"Yuhui"},{"full_name":"Freunberger, Stefan Alexander","id":"A8CA28E6-CE23-11E9-AD2D-EC27E6697425","orcid":"0000-0003-2902-5319","first_name":"Stefan Alexander","last_name":"Freunberger"},{"full_name":"Peng, Zhangquan","last_name":"Peng","first_name":"Zhangquan"},{"first_name":"Fanny","last_name":"Bardé","full_name":"Bardé, Fanny"},{"last_name":"Bruce","first_name":"Peter G.","full_name":"Bruce, Peter G."}],"publisher":"ACS","intvolume":" 134","title":"Li–O2 battery with a dimethylformamide electrolyte","status":"public","publication_status":"published","_id":"7311","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2012","article_processing_charge":"No","publication_identifier":{"issn":["0002-7863","1520-5126"]},"month":"04","day":"19","language":[{"iso":"eng"}],"doi":"10.1021/ja302178w","date_published":"2012-04-19T00:00:00Z","page":"7952-7957","quality_controlled":"1","article_type":"original","citation":{"ama":"Chen Y, Freunberger SA, Peng Z, Bardé F, Bruce PG. Li–O2 battery with a dimethylformamide electrolyte. Journal of the American Chemical Society. 2012;134(18):7952-7957. doi:10.1021/ja302178w","apa":"Chen, Y., Freunberger, S. A., Peng, Z., Bardé, F., & Bruce, P. G. (2012). Li–O2 battery with a dimethylformamide electrolyte. Journal of the American Chemical Society. ACS. https://doi.org/10.1021/ja302178w","ieee":"Y. Chen, S. A. Freunberger, Z. Peng, F. Bardé, and P. G. Bruce, “Li–O2 battery with a dimethylformamide electrolyte,” Journal of the American Chemical Society, vol. 134, no. 18. ACS, pp. 7952–7957, 2012.","ista":"Chen Y, Freunberger SA, Peng Z, Bardé F, Bruce PG. 2012. Li–O2 battery with a dimethylformamide electrolyte. Journal of the American Chemical Society. 134(18), 7952–7957.","short":"Y. Chen, S.A. Freunberger, Z. Peng, F. Bardé, P.G. Bruce, Journal of the American Chemical Society 134 (2012) 7952–7957.","mla":"Chen, Yuhui, et al. “Li–O2 Battery with a Dimethylformamide Electrolyte.” Journal of the American Chemical Society, vol. 134, no. 18, ACS, 2012, pp. 7952–57, doi:10.1021/ja302178w.","chicago":"Chen, Yuhui, Stefan Alexander Freunberger, Zhangquan Peng, Fanny Bardé, and Peter G. Bruce. “Li–O2 Battery with a Dimethylformamide Electrolyte.” Journal of the American Chemical Society. ACS, 2012. https://doi.org/10.1021/ja302178w."},"publication":"Journal of the American Chemical Society"},{"author":[{"full_name":"Tollinger, Martin","last_name":"Tollinger","first_name":"Martin"},{"last_name":"Sivertsen","first_name":"Astrid C.","full_name":"Sivertsen, Astrid C."},{"last_name":"Meier","first_name":"Beat H.","full_name":"Meier, Beat H."},{"last_name":"Ernst","first_name":"Matthias","full_name":"Ernst, Matthias"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul"}],"date_created":"2020-09-18T10:10:20Z","date_updated":"2021-01-12T08:19:27Z","volume":134,"oa_version":"None","_id":"8465","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2012","status":"public","title":"Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy","publication_status":"published","publisher":"American Chemical Society","intvolume":" 134","abstract":[{"text":"We demonstrate that conformational exchange processes in proteins on microsecond-to-millisecond time scales can be detected and quantified by solid-state NMR spectroscopy. We show two independent approaches that measure the effect of conformational exchange on transverse relaxation parameters, namely Carr–Purcell–Meiboom–Gill relaxation-dispersion experiments and measurement of differential multiple-quantum coherence decay. Long coherence lifetimes, as required for these experiments, are achieved by the use of highly deuterated samples and fast magic-angle spinning. The usefulness of the approaches is demonstrated by application to microcrystalline ubiquitin. We detect a conformational exchange process in a region of the protein for which dynamics have also been observed in solution. Interestingly, quantitative analysis of the data reveals that the exchange process is more than 1 order of magnitude slower than in solution, and this points to the impact of the crystalline environment on free energy barriers.","lang":"eng"}],"issue":"36","extern":"1","type":"journal_article","doi":"10.1021/ja303591y","date_published":"2012-08-21T00:00:00Z","language":[{"iso":"eng"}],"publication":"Journal of the American Chemical Society","citation":{"apa":"Tollinger, M., Sivertsen, A. C., Meier, B. H., Ernst, M., & Schanda, P. (2012). Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja303591y","ieee":"M. Tollinger, A. C. Sivertsen, B. H. Meier, M. Ernst, and P. Schanda, “Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy,” Journal of the American Chemical Society, vol. 134, no. 36. American Chemical Society, pp. 14800–14807, 2012.","ista":"Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. 2012. Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society. 134(36), 14800–14807.","ama":"Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society. 2012;134(36):14800-14807. doi:10.1021/ja303591y","chicago":"Tollinger, Martin, Astrid C. Sivertsen, Beat H. Meier, Matthias Ernst, and Paul Schanda. “Site-Resolved Measurement of Microsecond-to-Millisecond Conformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy.” Journal of the American Chemical Society. American Chemical Society, 2012. https://doi.org/10.1021/ja303591y.","short":"M. Tollinger, A.C. Sivertsen, B.H. Meier, M. Ernst, P. Schanda, Journal of the American Chemical Society 134 (2012) 14800–14807.","mla":"Tollinger, Martin, et al. “Site-Resolved Measurement of Microsecond-to-Millisecond Conformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy.” Journal of the American Chemical Society, vol. 134, no. 36, American Chemical Society, 2012, pp. 14800–07, doi:10.1021/ja303591y."},"quality_controlled":"1","article_type":"original","page":"14800-14807","day":"21","month":"08","publication_identifier":{"issn":["0002-7863","1520-5126"]},"article_processing_charge":"No"},{"abstract":[{"lang":"eng","text":"Recent advances in NMR spectroscopy and the availability of high magnetic field strengths now offer the possibility to record real-time 3D NMR spectra of short-lived protein states, e.g., states that become transiently populated during protein folding. Here we present a strategy for obtaining sequential NMR assignments as well as atom-resolved information on structural and dynamic features within a folding intermediate of the amyloidogenic protein β2-microglobulin that has a half-lifetime of only 20 min."}],"issue":"19","extern":"1","type":"journal_article","author":[{"full_name":"Rennella, Enrico","last_name":"Rennella","first_name":"Enrico"},{"full_name":"Cutuil, Thomas","first_name":"Thomas","last_name":"Cutuil"},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"first_name":"Isabel","last_name":"Ayala","full_name":"Ayala, Isabel"},{"full_name":"Forge, Vincent","last_name":"Forge","first_name":"Vincent"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}],"date_created":"2020-09-18T10:10:28Z","date_updated":"2021-01-12T08:19:28Z","volume":134,"oa_version":"None","year":"2012","_id":"8466","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","title":"Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate","status":"public","publisher":"American Chemical Society","intvolume":" 134","month":"05","day":"03","publication_identifier":{"issn":["0002-7863","1520-5126"]},"article_processing_charge":"No","date_published":"2012-05-03T00:00:00Z","doi":"10.1021/ja302598j","language":[{"iso":"eng"}],"publication":"Journal of the American Chemical Society","citation":{"ama":"Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate. Journal of the American Chemical Society. 2012;134(19):8066-8069. doi:10.1021/ja302598j","apa":"Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Forge, V., & Brutscher, B. (2012). Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja302598j","ieee":"E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, and B. Brutscher, “Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate,” Journal of the American Chemical Society, vol. 134, no. 19. American Chemical Society, pp. 8066–8069, 2012.","ista":"Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. 2012. Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate. Journal of the American Chemical Society. 134(19), 8066–8069.","short":"E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, B. Brutscher, Journal of the American Chemical Society 134 (2012) 8066–8069.","mla":"Rennella, Enrico, et al. “Real-Time NMR Characterization of Structure and Dynamics in a Transiently Populated Protein Folding Intermediate.” Journal of the American Chemical Society, vol. 134, no. 19, American Chemical Society, 2012, pp. 8066–69, doi:10.1021/ja302598j.","chicago":"Rennella, Enrico, Thomas Cutuil, Paul Schanda, Isabel Ayala, Vincent Forge, and Bernhard Brutscher. “Real-Time NMR Characterization of Structure and Dynamics in a Transiently Populated Protein Folding Intermediate.” Journal of the American Chemical Society. American Chemical Society, 2012. https://doi.org/10.1021/ja302598j."},"quality_controlled":"1","article_type":"original","page":"8066-8069"},{"date_updated":"2021-01-12T08:13:00Z","date_created":"2020-01-15T12:20:43Z","oa_version":"None","volume":133,"author":[{"last_name":"Freunberger","first_name":"Stefan Alexander","orcid":"0000-0003-2902-5319","id":"A8CA28E6-CE23-11E9-AD2D-EC27E6697425","full_name":"Freunberger, Stefan Alexander"},{"full_name":"Chen, Yuhui","first_name":"Yuhui","last_name":"Chen"},{"full_name":"Peng, Zhangquan","last_name":"Peng","first_name":"Zhangquan"},{"full_name":"Griffin, John M.","last_name":"Griffin","first_name":"John M."},{"last_name":"Hardwick","first_name":"Laurence J.","full_name":"Hardwick, Laurence J."},{"first_name":"Fanny","last_name":"Bardé","full_name":"Bardé, Fanny"},{"full_name":"Novák, Petr","first_name":"Petr","last_name":"Novák"},{"first_name":"Peter G.","last_name":"Bruce","full_name":"Bruce, Peter G."}],"title":"Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes","publication_status":"published","status":"public","publisher":"ACS","intvolume":" 133","_id":"7316","year":"2011","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","abstract":[{"text":"The nonaqueous rechargeable lithium–O2 battery containing an alkyl carbonate electrolyte discharges by formation of C3H6(OCO2Li)2, Li2CO3, HCO2Li, CH3CO2Li, CO2, and H2O at the cathode, due to electrolyte decomposition. Charging involves oxidation of C3H6(OCO2Li)2, Li2CO3, HCO2Li, CH3CO2Li accompanied by CO2 and H2O evolution. Mechanisms are proposed for the reactions on discharge and charge. The different pathways for discharge and charge are consistent with the widely observed voltage gap in Li–O2 cells. Oxidation of C3H6(OCO2Li)2 involves terminal carbonate groups leaving behind the OC3H6O moiety that reacts to form a thick gel on the Li anode. Li2CO3, HCO2Li, CH3CO2Li, and C3H6(OCO2Li)2 accumulate in the cathode on cycling correlating with capacity fading and cell failure. The latter is compounded by continuous consumption of the electrolyte on each discharge.","lang":"eng"}],"issue":"20","type":"journal_article","language":[{"iso":"eng"}],"date_published":"2011-04-27T00:00:00Z","doi":"10.1021/ja2021747","article_type":"original","quality_controlled":"1","page":"8040-8047","publication":"Journal of the American Chemical Society","citation":{"chicago":"Freunberger, Stefan Alexander, Yuhui Chen, Zhangquan Peng, John M. Griffin, Laurence J. Hardwick, Fanny Bardé, Petr Novák, and Peter G. Bruce. “Reactions in the Rechargeable Lithium–O2 Battery with Alkyl Carbonate Electrolytes.” Journal of the American Chemical Society. ACS, 2011. https://doi.org/10.1021/ja2021747.","mla":"Freunberger, Stefan Alexander, et al. “Reactions in the Rechargeable Lithium–O2 Battery with Alkyl Carbonate Electrolytes.” Journal of the American Chemical Society, vol. 133, no. 20, ACS, 2011, pp. 8040–47, doi:10.1021/ja2021747.","short":"S.A. Freunberger, Y. Chen, Z. Peng, J.M. Griffin, L.J. Hardwick, F. Bardé, P. Novák, P.G. Bruce, Journal of the American Chemical Society 133 (2011) 8040–8047.","ista":"Freunberger SA, Chen Y, Peng Z, Griffin JM, Hardwick LJ, Bardé F, Novák P, Bruce PG. 2011. Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes. Journal of the American Chemical Society. 133(20), 8040–8047.","ieee":"S. A. Freunberger et al., “Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes,” Journal of the American Chemical Society, vol. 133, no. 20. ACS, pp. 8040–8047, 2011.","apa":"Freunberger, S. A., Chen, Y., Peng, Z., Griffin, J. M., Hardwick, L. J., Bardé, F., … Bruce, P. G. (2011). Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes. Journal of the American Chemical Society. ACS. https://doi.org/10.1021/ja2021747","ama":"Freunberger SA, Chen Y, Peng Z, et al. Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes. Journal of the American Chemical Society. 2011;133(20):8040-8047. doi:10.1021/ja2021747"},"month":"04","day":"27","publication_identifier":{"issn":["0002-7863","1520-5126"]},"article_processing_charge":"No"},{"date_created":"2020-09-18T10:11:13Z","date_updated":"2021-01-12T08:19:30Z","oa_version":"None","volume":132,"author":[{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul"},{"full_name":"Meier, Beat H.","last_name":"Meier","first_name":"Beat H."},{"first_name":"Matthias","last_name":"Ernst","full_name":"Ernst, Matthias"}],"publication_status":"published","title":"Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy","status":"public","publisher":"American Chemical Society","intvolume":" 132","year":"2010","_id":"8472","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","abstract":[{"lang":"eng","text":"Characterization of protein dynamics by solid-state NMR spectroscopy requires robust and accurate measurement protocols, which are not yet fully developed. In this study, we investigate the backbone dynamics of microcrystalline ubiquitin using different approaches. A rotational-echo double-resonance type (REDOR-type) methodology allows one to accurately measure 1H−15N order parameters in highly deuterated samples. We show that the systematic errors in the REDOR experiment are as low as 1% or even less, giving access to accurate data for the amplitudes of backbone mobility. Combining such dipolar-coupling-derived order parameters with autocorrelated and cross-correlated 15N relaxation rates, we are able to quantitate amplitudes and correlation times of backbone dynamics on picosecond and nanosecond time scales in a residue-resolved manner. While the mobility on picosecond time scales appears to have rather uniform amplitude throughout the protein, we unambiguously identify and quantitate nanosecond mobility with order parameters S2 as low as 0.8 in some regions of the protein, where nanosecond dynamics has also been revealed in solution state. The methodology used here, a combination of accurate dipolar-coupling measurements and different relaxation parameters, yields details about dynamics on different time scales and can be applied to solid protein samples such as amyloid fibrils or membrane proteins."}],"issue":"45","type":"journal_article","language":[{"iso":"eng"}],"date_published":"2010-10-26T00:00:00Z","doi":"10.1021/ja100726a","quality_controlled":"1","article_type":"original","page":"15957-15967","publication":"Journal of the American Chemical Society","citation":{"short":"P. Schanda, B.H. Meier, M. Ernst, Journal of the American Chemical Society 132 (2010) 15957–15967.","mla":"Schanda, Paul, et al. “Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.” Journal of the American Chemical Society, vol. 132, no. 45, American Chemical Society, 2010, pp. 15957–67, doi:10.1021/ja100726a.","chicago":"Schanda, Paul, Beat H. Meier, and Matthias Ernst. “Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.” Journal of the American Chemical Society. American Chemical Society, 2010. https://doi.org/10.1021/ja100726a.","ama":"Schanda P, Meier BH, Ernst M. Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal of the American Chemical Society. 2010;132(45):15957-15967. doi:10.1021/ja100726a","apa":"Schanda, P., Meier, B. H., & Ernst, M. (2010). Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja100726a","ieee":"P. Schanda, B. H. Meier, and M. Ernst, “Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy,” Journal of the American Chemical Society, vol. 132, no. 45. American Chemical Society, pp. 15957–15967, 2010.","ista":"Schanda P, Meier BH, Ernst M. 2010. Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal of the American Chemical Society. 132(45), 15957–15967."},"day":"26","month":"10","publication_identifier":{"issn":["0002-7863","1520-5126"]},"article_processing_charge":"No"},{"citation":{"chicago":"Brüschweiler, Sven, Paul Schanda, Karin Kloiber, Bernhard Brutscher, Georg Kontaxis, Robert Konrat, and Martin Tollinger. “Direct Observation of the Dynamic Process Underlying Allosteric Signal Transmission.” Journal of the American Chemical Society. American Chemical Society, 2009. https://doi.org/10.1021/ja809947w.","short":"S. Brüschweiler, P. Schanda, K. Kloiber, B. Brutscher, G. Kontaxis, R. Konrat, M. Tollinger, Journal of the American Chemical Society 131 (2009) 3063–3068.","mla":"Brüschweiler, Sven, et al. “Direct Observation of the Dynamic Process Underlying Allosteric Signal Transmission.” Journal of the American Chemical Society, vol. 131, no. 8, American Chemical Society, 2009, pp. 3063–68, doi:10.1021/ja809947w.","ieee":"S. Brüschweiler et al., “Direct observation of the dynamic process underlying allosteric signal transmission,” Journal of the American Chemical Society, vol. 131, no. 8. American Chemical Society, pp. 3063–3068, 2009.","apa":"Brüschweiler, S., Schanda, P., Kloiber, K., Brutscher, B., Kontaxis, G., Konrat, R., & Tollinger, M. (2009). Direct observation of the dynamic process underlying allosteric signal transmission. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja809947w","ista":"Brüschweiler S, Schanda P, Kloiber K, Brutscher B, Kontaxis G, Konrat R, Tollinger M. 2009. Direct observation of the dynamic process underlying allosteric signal transmission. Journal of the American Chemical Society. 131(8), 3063–3068.","ama":"Brüschweiler S, Schanda P, Kloiber K, et al. Direct observation of the dynamic process underlying allosteric signal transmission. Journal of the American Chemical Society. 2009;131(8):3063-3068. doi:10.1021/ja809947w"},"publication":"Journal of the American Chemical Society","page":"3063-3068","article_type":"original","quality_controlled":"1","date_published":"2009-02-09T00:00:00Z","doi":"10.1021/ja809947w","language":[{"iso":"eng"}],"article_processing_charge":"No","publication_identifier":{"issn":["0002-7863","1520-5126"]},"month":"02","day":"09","_id":"8478","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2009","intvolume":" 131","publisher":"American Chemical Society","status":"public","title":"Direct observation of the dynamic process underlying allosteric signal transmission","publication_status":"published","author":[{"first_name":"Sven","last_name":"Brüschweiler","full_name":"Brüschweiler, Sven"},{"last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"},{"full_name":"Kloiber, Karin","first_name":"Karin","last_name":"Kloiber"},{"full_name":"Brutscher, Bernhard","last_name":"Brutscher","first_name":"Bernhard"},{"full_name":"Kontaxis, Georg","first_name":"Georg","last_name":"Kontaxis"},{"full_name":"Konrat, Robert","first_name":"Robert","last_name":"Konrat"},{"full_name":"Tollinger, Martin","last_name":"Tollinger","first_name":"Martin"}],"volume":131,"oa_version":"None","date_updated":"2021-01-12T08:19:33Z","date_created":"2020-09-18T10:12:14Z","type":"journal_article","issue":"8","abstract":[{"text":"Allosteric regulation is an effective mechanism of control in biological processes. In allosteric proteins a signal originating at one site in the molecule is communicated through the protein structure to trigger a specific response at a remote site. Using NMR relaxation dispersion techniques we directly observe the dynamic process through which the KIX domain of CREB binding protein communicates allosteric information between binding sites. KIX mediates cooperativity between pairs of transcription factors through binding to two distinct interaction surfaces in an allosteric manner. We show that binding the activation domain of the mixed lineage leukemia (MLL) transcription factor to KIX induces a redistribution of the relative populations of KIX conformations toward a high-energy state in which the allosterically activated second binding site is already preformed, consistent with the Monod−Wyman−Changeux (WMC) model of allostery. The structural rearrangement process that links the two conformers and by which allosteric information is communicated occurs with a time constant of 3 ms at 27 °C. Our dynamic NMR data reveal that an evolutionarily conserved network of hydrophobic amino acids constitutes the pathway through which information is transmitted.","lang":"eng"}],"extern":"1"},{"article_processing_charge":"No","publication_identifier":{"issn":["0002-7863","1520-5126"]},"month":"06","day":"01","doi":"10.1021/ja901633y","date_published":"2009-06-01T00:00:00Z","language":[{"iso":"eng"}],"citation":{"mla":"Farjon, Jonathan, et al. “Longitudinal-Relaxation-Enhanced NMR Experiments for the Study of Nucleic Acids in Solution.” Journal of the American Chemical Society, vol. 131, no. 24, American Chemical Society, 2009, pp. 8571–77, doi:10.1021/ja901633y.","short":"J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, B. Brutscher, Journal of the American Chemical Society 131 (2009) 8571–8577.","chicago":"Farjon, Jonathan, Jérôme Boisbouvier, Paul Schanda, Arthur Pardi, Jean-Pierre Simorre, and Bernhard Brutscher. “Longitudinal-Relaxation-Enhanced NMR Experiments for the Study of Nucleic Acids in Solution.” Journal of the American Chemical Society. American Chemical Society, 2009. https://doi.org/10.1021/ja901633y.","ama":"Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. Journal of the American Chemical Society. 2009;131(24):8571-8577. doi:10.1021/ja901633y","ista":"Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. 2009. Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. Journal of the American Chemical Society. 131(24), 8571–8577.","ieee":"J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, and B. Brutscher, “Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution,” Journal of the American Chemical Society, vol. 131, no. 24. American Chemical Society, pp. 8571–8577, 2009.","apa":"Farjon, J., Boisbouvier, J., Schanda, P., Pardi, A., Simorre, J.-P., & Brutscher, B. (2009). Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja901633y"},"publication":"Journal of the American Chemical Society","page":"8571-8577","article_type":"original","quality_controlled":"1","issue":"24","abstract":[{"text":"Atomic-resolution information on the structure and dynamics of nucleic acids is essential for a better understanding of the mechanistic basis of many cellular processes. NMR spectroscopy is a powerful method for studying the structure and dynamics of nucleic acids; however, solution NMR studies are currently limited to relatively small nucleic acids at high concentrations. Thus, technological and methodological improvements that increase the experimental sensitivity and spectral resolution of NMR spectroscopy are required for studies of larger nucleic acids or protein−nucleic acid complexes. Here we introduce a series of imino-proton-detected NMR experiments that yield an over 2-fold increase in sensitivity compared to conventional pulse schemes. These methods can be applied to the detection of base pair interactions, RNA−ligand titration experiments, measurement of residual dipolar 15N−1H couplings, and direct measurements of conformational transitions. These NMR experiments employ longitudinal spin relaxation enhancement techniques that have proven useful in protein NMR spectroscopy. The performance of these new experiments is demonstrated for a 10 kDa TAR-TAR*GA RNA kissing complex and a 26 kDa tRNA.","lang":"eng"}],"extern":"1","type":"journal_article","author":[{"full_name":"Farjon, Jonathan","last_name":"Farjon","first_name":"Jonathan"},{"last_name":"Boisbouvier","first_name":"Jérôme","full_name":"Boisbouvier, Jérôme"},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"first_name":"Arthur","last_name":"Pardi","full_name":"Pardi, Arthur"},{"full_name":"Simorre, Jean-Pierre","last_name":"Simorre","first_name":"Jean-Pierre"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}],"oa_version":"None","volume":131,"date_updated":"2021-01-12T08:19:32Z","date_created":"2020-09-18T10:11:49Z","year":"2009","_id":"8476","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"American Chemical Society","intvolume":" 131","publication_status":"published","title":"Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution","status":"public"},{"issue":"10","abstract":[{"text":"An optimized NMR experiment that combines the advantages of methyl-TROSY and SOFAST-HMQC has been developed. It allows the recording of high quality methyl 1H−13C correlation spectra of protein assemblies of several hundreds of kDa in a few seconds. The SOFAST-methyl-TROSY-based experiment offers completely new opportunities for the study of structural and dynamic changes occurring in molecular nanomachines while they perform their biological function in vitro.","lang":"eng"}],"extern":"1","type":"journal_article","author":[{"full_name":"Amero, Carlos","first_name":"Carlos","last_name":"Amero"},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda"},{"full_name":"Durá, M. Asunción","last_name":"Durá","first_name":"M. Asunción"},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"last_name":"Marion","first_name":"Dominique","full_name":"Marion, Dominique"},{"full_name":"Franzetti, Bruno","first_name":"Bruno","last_name":"Franzetti"},{"first_name":"Bernhard","last_name":"Brutscher","full_name":"Brutscher, Bernhard"},{"first_name":"Jérôme","last_name":"Boisbouvier","full_name":"Boisbouvier, Jérôme"}],"oa_version":"None","volume":131,"date_updated":"2021-01-12T08:19:32Z","date_created":"2020-09-18T10:12:01Z","year":"2009","_id":"8477","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"American Chemical Society","intvolume":" 131","publication_status":"published","status":"public","title":"Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies","article_processing_charge":"No","publication_identifier":{"issn":["0002-7863","1520-5126"]},"month":"02","day":"25","doi":"10.1021/ja809880p","date_published":"2009-02-25T00:00:00Z","language":[{"iso":"eng"}],"citation":{"ama":"Amero C, Schanda P, Durá MA, et al. Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. Journal of the American Chemical Society. 2009;131(10):3448-3449. doi:10.1021/ja809880p","ista":"Amero C, Schanda P, Durá MA, Ayala I, Marion D, Franzetti B, Brutscher B, Boisbouvier J. 2009. Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. Journal of the American Chemical Society. 131(10), 3448–3449.","ieee":"C. Amero et al., “Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies,” Journal of the American Chemical Society, vol. 131, no. 10. American Chemical Society, pp. 3448–3449, 2009.","apa":"Amero, C., Schanda, P., Durá, M. A., Ayala, I., Marion, D., Franzetti, B., … Boisbouvier, J. (2009). Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja809880p","mla":"Amero, Carlos, et al. “Fast Two-Dimensional NMR Spectroscopy of High Molecular Weight Protein Assemblies.” Journal of the American Chemical Society, vol. 131, no. 10, American Chemical Society, 2009, pp. 3448–49, doi:10.1021/ja809880p.","short":"C. Amero, P. Schanda, M.A. Durá, I. Ayala, D. Marion, B. Franzetti, B. Brutscher, J. Boisbouvier, Journal of the American Chemical Society 131 (2009) 3448–3449.","chicago":"Amero, Carlos, Paul Schanda, M. Asunción Durá, Isabel Ayala, Dominique Marion, Bruno Franzetti, Bernhard Brutscher, and Jérôme Boisbouvier. “Fast Two-Dimensional NMR Spectroscopy of High Molecular Weight Protein Assemblies.” Journal of the American Chemical Society. American Chemical Society, 2009. https://doi.org/10.1021/ja809880p."},"publication":"Journal of the American Chemical Society","page":"3448-3449","article_type":"original","quality_controlled":"1"},{"author":[{"first_name":"Maayan","last_name":"Gal","full_name":"Gal, Maayan"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"},{"full_name":"Frydman, Lucio","first_name":"Lucio","last_name":"Frydman"}],"date_updated":"2021-01-12T08:19:37Z","date_created":"2020-09-18T10:13:27Z","oa_version":"None","volume":129,"_id":"8487","year":"2007","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","publication_status":"published","title":"UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates","intvolume":" 129","publisher":"American Chemical Society","abstract":[{"lang":"eng","text":"Following unidirectional biophysical events such as the folding of proteins or the equilibration of binding interactions, requires experimental methods that yield information at both atomic-level resolution and at high repetition rates. Toward this end a number of different approaches enabling the rapid acquisition of 2D NMR spectra have been recently introduced, including spatially encoded “ultrafast” 2D NMR spectroscopy and SOFAST HMQC NMR. Whereas the former accelerates acquisitions by reducing the number of scans that are necessary for completing arbitrary 2D NMR experiments, the latter operates by reducing the delay between consecutive scans while preserving sensitivity. Given the complementarities between these two approaches it seems natural to combine them into a single tool, enabling the acquisition of full 2D protein NMR spectra at high repetition rates. We demonstrate here this capability with the introduction of “ultraSOFAST” HMQC NMR, a spatially encoded and relaxation-optimized approach that can provide 2D protein correlation spectra at ∼1 s repetition rates for samples in the ∼2 mM concentration range. The principles, relative advantages, and current limitations of this new approach are discussed, and its application is exemplified with a study of the fast hydrogen−deuterium exchange characterizing amide sites in Ubiquitin."}],"issue":"5","extern":"1","type":"journal_article","doi":"10.1021/ja066915g","date_published":"2007-01-10T00:00:00Z","language":[{"iso":"eng"}],"publication":"Journal of the American Chemical Society","citation":{"apa":"Gal, M., Schanda, P., Brutscher, B., & Frydman, L. (2007). UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja066915g","ieee":"M. Gal, P. Schanda, B. Brutscher, and L. Frydman, “UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates,” Journal of the American Chemical Society, vol. 129, no. 5. American Chemical Society, pp. 1372–1377, 2007.","ista":"Gal M, Schanda P, Brutscher B, Frydman L. 2007. UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American Chemical Society. 129(5), 1372–1377.","ama":"Gal M, Schanda P, Brutscher B, Frydman L. UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American Chemical Society. 2007;129(5):1372-1377. doi:10.1021/ja066915g","chicago":"Gal, Maayan, Paul Schanda, Bernhard Brutscher, and Lucio Frydman. “UltraSOFAST HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz Rates.” Journal of the American Chemical Society. American Chemical Society, 2007. https://doi.org/10.1021/ja066915g.","short":"M. Gal, P. Schanda, B. Brutscher, L. Frydman, Journal of the American Chemical Society 129 (2007) 1372–1377.","mla":"Gal, Maayan, et al. “UltraSOFAST HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz Rates.” Journal of the American Chemical Society, vol. 129, no. 5, American Chemical Society, 2007, pp. 1372–77, doi:10.1021/ja066915g."},"article_type":"original","quality_controlled":"1","page":"1372-1377","day":"10","month":"01","article_processing_charge":"No","publication_identifier":{"issn":["0002-7863","1520-5126"]},"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"]},{"abstract":[{"lang":"eng","text":"A technique is described that allows reducing acquisition times of multidimensional NMR experiments by extensive spectral folding. The method is simple and has many interesting applications for NMR studies of molecular structure, dynamics, and kinetics."}],"issue":"10","extern":"1","type":"journal_article","author":[{"full_name":"Lescop, Ewen","last_name":"Lescop","first_name":"Ewen"},{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul"},{"last_name":"Rasia","first_name":"Rodolfo","full_name":"Rasia, Rodolfo"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}],"date_created":"2020-09-18T10:13:21Z","date_updated":"2021-01-12T08:19:36Z","oa_version":"None","volume":129,"year":"2007","_id":"8486","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy","status":"public","publication_status":"published","intvolume":" 129","publisher":"American Chemical Society","day":"17","month":"02","article_processing_charge":"No","publication_identifier":{"issn":["0002-7863","1520-5126"]},"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"doi":"10.1021/ja068949u","date_published":"2007-02-17T00:00:00Z","language":[{"iso":"eng"}],"publication":"Journal of the American Chemical Society","citation":{"chicago":"Lescop, Ewen, Paul Schanda, Rodolfo Rasia, and Bernhard Brutscher. “Automated Spectral Compression for Fast Multidimensional NMR and Increased Time Resolution in Real-Time NMR Spectroscopy.” Journal of the American Chemical Society. American Chemical Society, 2007. https://doi.org/10.1021/ja068949u.","mla":"Lescop, Ewen, et al. “Automated Spectral Compression for Fast Multidimensional NMR and Increased Time Resolution in Real-Time NMR Spectroscopy.” Journal of the American Chemical Society, vol. 129, no. 10, American Chemical Society, 2007, pp. 2756–57, doi:10.1021/ja068949u.","short":"E. Lescop, P. Schanda, R. Rasia, B. Brutscher, Journal of the American Chemical Society 129 (2007) 2756–2757.","ista":"Lescop E, Schanda P, Rasia R, Brutscher B. 2007. Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. Journal of the American Chemical Society. 129(10), 2756–2757.","apa":"Lescop, E., Schanda, P., Rasia, R., & Brutscher, B. (2007). Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja068949u","ieee":"E. Lescop, P. Schanda, R. Rasia, and B. Brutscher, “Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy,” Journal of the American Chemical Society, vol. 129, no. 10. American Chemical Society, pp. 2756–2757, 2007.","ama":"Lescop E, Schanda P, Rasia R, Brutscher B. Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. Journal of the American Chemical Society. 2007;129(10):2756-2757. doi:10.1021/ja068949u"},"article_type":"original","quality_controlled":"1","page":"2756-2757"},{"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"publication_identifier":{"issn":["0002-7863","1520-5126"]},"article_processing_charge":"No","day":"21","month":"06","citation":{"ieee":"P. Schanda, H. Van Melckebeke, and B. Brutscher, “Speeding up three-dimensional protein NMR experiments to a few minutes,” Journal of the American Chemical Society, vol. 128, no. 28. American Chemical Society, pp. 9042–9043, 2006.","apa":"Schanda, P., Van Melckebeke, H., & Brutscher, B. (2006). Speeding up three-dimensional protein NMR experiments to a few minutes. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja062025p","ista":"Schanda P, Van Melckebeke H, Brutscher B. 2006. Speeding up three-dimensional protein NMR experiments to a few minutes. Journal of the American Chemical Society. 128(28), 9042–9043.","ama":"Schanda P, Van Melckebeke H, Brutscher B. Speeding up three-dimensional protein NMR experiments to a few minutes. Journal of the American Chemical Society. 2006;128(28):9042-9043. doi:10.1021/ja062025p","chicago":"Schanda, Paul, Hélène Van Melckebeke, and Bernhard Brutscher. “Speeding up Three-Dimensional Protein NMR Experiments to a Few Minutes.” Journal of the American Chemical Society. American Chemical Society, 2006. https://doi.org/10.1021/ja062025p.","short":"P. Schanda, H. Van Melckebeke, B. Brutscher, Journal of the American Chemical Society 128 (2006) 9042–9043.","mla":"Schanda, Paul, et al. “Speeding up Three-Dimensional Protein NMR Experiments to a Few Minutes.” Journal of the American Chemical Society, vol. 128, no. 28, American Chemical Society, 2006, pp. 9042–43, doi:10.1021/ja062025p."},"publication":"Journal of the American Chemical Society","page":"9042-9043","quality_controlled":"1","article_type":"original","doi":"10.1021/ja062025p","date_published":"2006-06-21T00:00:00Z","language":[{"iso":"eng"}],"type":"journal_article","issue":"28","abstract":[{"text":"We demonstrate for different protein samples that three-dimensional HNCO and HNCA correlation spectra may be recorded in a few minutes acquisition time using the band-selective excitation short-transient sequences presented here. This opens new perspectives for the NMR structural investigation of unstable protein samples and real-time site-resolved studies of protein kinetics.","lang":"eng"}],"extern":"1","year":"2006","_id":"8488","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","intvolume":" 128","publisher":"American Chemical Society","status":"public","title":"Speeding up three-dimensional protein NMR experiments to a few minutes","publication_status":"published","author":[{"full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"},{"full_name":"Van Melckebeke, Hélène","last_name":"Van Melckebeke","first_name":"Hélène"},{"full_name":"Brutscher, Bernhard","last_name":"Brutscher","first_name":"Bernhard"}],"oa_version":"None","volume":128,"date_created":"2020-09-18T10:13:36Z","date_updated":"2021-01-12T08:19:37Z"},{"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"month":"05","day":"14","publication_identifier":{"issn":["0002-7863","1520-5126"]},"article_processing_charge":"No","quality_controlled":"1","article_type":"original","page":"8014-8015","publication":"Journal of the American Chemical Society","citation":{"mla":"Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds.” Journal of the American Chemical Society, vol. 127, no. 22, American Chemical Society, 2005, pp. 8014–15, doi:10.1021/ja051306e.","short":"P. Schanda, B. Brutscher, Journal of the American Chemical Society 127 (2005) 8014–8015.","chicago":"Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds.” Journal of the American Chemical Society. American Chemical Society, 2005. https://doi.org/10.1021/ja051306e.","ama":"Schanda P, Brutscher B. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. 2005;127(22):8014-8015. doi:10.1021/ja051306e","ista":"Schanda P, Brutscher B. 2005. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. 127(22), 8014–8015.","ieee":"P. Schanda and B. Brutscher, “Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds,” Journal of the American Chemical Society, vol. 127, no. 22. American Chemical Society, pp. 8014–8015, 2005.","apa":"Schanda, P., & Brutscher, B. (2005). Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja051306e"},"language":[{"iso":"eng"}],"doi":"10.1021/ja051306e","date_published":"2005-05-14T00:00:00Z","type":"journal_article","extern":"1","abstract":[{"text":"We demonstrate for different protein samples that 2D 1H−15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle short-transient heteronuclear multiple quantum coherence experiment. This has enabled us to measure fast hydrogen−deuterium exchange rate constants along the backbone of a small globular protein fragment by real-time 2D NMR.","lang":"eng"}],"issue":"22","title":"Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds","publication_status":"published","status":"public","publisher":"American Chemical Society","intvolume":" 127","_id":"8492","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2005","date_created":"2020-09-18T10:14:05Z","date_updated":"2021-01-12T08:19:39Z","oa_version":"None","volume":127,"author":[{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}]}]