[{"type":"journal_article","keyword":["Physical and Theoretical Chemistry","Materials Chemistry","Surfaces","Coatings and Films"],"date_created":"2020-09-18T10:07:07Z","intvolume":"       120","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"text":"Transverse relaxation rate measurements in magic-angle spinning solid-state nuclear magnetic resonance provide information about molecular motions occurring on nanosecond-to-millisecond (ns–ms) time scales. The measurement of heteronuclear (13C, 15N) relaxation rate constants in the presence of a spin-lock radiofrequency field (R1ρ relaxation) provides access to such motions, and an increasing number of studies involving R1ρ relaxation in proteins have been reported. However, two factors that influence the observed relaxation rate constants have so far been neglected, namely, (1) the role of CSA/dipolar cross-correlated relaxation (CCR) and (2) the impact of fast proton spin flips (i.e., proton spin diffusion and relaxation). We show that CSA/D CCR in R1ρ experiments is measurable and that the CCR rate constant depends on ns–ms motions; it can thus provide insight into dynamics. We find that proton spin diffusion attenuates this CCR due to its decoupling effect on the doublet components. For measurements of dynamics, the use of R1ρ rate constants has practical advantages over the use of CCR rates, and this article reveals factors that have so far been disregarded and which are important for accurate measurements and interpretation.","lang":"eng"}],"publication":"The Journal of Physical Chemistry B","date_published":"2016-08-08T00:00:00Z","volume":120,"status":"public","quality_controlled":"1","oa_version":"None","publication_status":"published","publisher":"American Chemical Society","article_type":"original","extern":"1","language":[{"iso":"eng"}],"day":"08","citation":{"chicago":"Kurauskas, Vilius, Emmanuelle Weber, Audrey Hessel, Isabel Ayala, Dominique Marion, and Paul Schanda. “Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning R1ρ NMR Measurements: Application to Protein Backbone Dynamics Measurements.” <i>The Journal of Physical Chemistry B</i>. American Chemical Society, 2016. <a href=\"https://doi.org/10.1021/acs.jpcb.6b06129\">https://doi.org/10.1021/acs.jpcb.6b06129</a>.","ieee":"V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, and P. Schanda, “Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements,” <i>The Journal of Physical Chemistry B</i>, vol. 120, no. 34. American Chemical Society, pp. 8905–8913, 2016.","mla":"Kurauskas, Vilius, et al. “Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning R1ρ NMR Measurements: Application to Protein Backbone Dynamics Measurements.” <i>The Journal of Physical Chemistry B</i>, vol. 120, no. 34, American Chemical Society, 2016, pp. 8905–13, doi:<a href=\"https://doi.org/10.1021/acs.jpcb.6b06129\">10.1021/acs.jpcb.6b06129</a>.","ama":"Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P. Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements. <i>The Journal of Physical Chemistry B</i>. 2016;120(34):8905-8913. doi:<a href=\"https://doi.org/10.1021/acs.jpcb.6b06129\">10.1021/acs.jpcb.6b06129</a>","ista":"Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P. 2016. Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements. The Journal of Physical Chemistry B. 120(34), 8905–8913.","short":"V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, P. Schanda, The Journal of Physical Chemistry B 120 (2016) 8905–8913.","apa":"Kurauskas, V., Weber, E., Hessel, A., Ayala, I., Marion, D., &#38; Schanda, P. (2016). Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements. <i>The Journal of Physical Chemistry B</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.jpcb.6b06129\">https://doi.org/10.1021/acs.jpcb.6b06129</a>"},"publication_identifier":{"issn":["1520-6106","1520-5207"]},"page":"8905-8913","author":[{"first_name":"Vilius","last_name":"Kurauskas","full_name":"Kurauskas, Vilius"},{"full_name":"Weber, Emmanuelle","first_name":"Emmanuelle","last_name":"Weber"},{"last_name":"Hessel","first_name":"Audrey","full_name":"Hessel, Audrey"},{"full_name":"Ayala, Isabel","last_name":"Ayala","first_name":"Isabel"},{"first_name":"Dominique","last_name":"Marion","full_name":"Marion, Dominique"},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul"}],"doi":"10.1021/acs.jpcb.6b06129","year":"2016","_id":"8453","title":"Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements","date_updated":"2021-01-12T08:19:22Z","month":"08","article_processing_charge":"No","issue":"34"},{"issue":"13","title":"Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations","_id":"7780","article_processing_charge":"No","month":"03","date_updated":"2021-01-12T08:15:29Z","page":"3332-3335","day":"13","publication_identifier":{"issn":["1520-6106","1520-5207"]},"citation":{"ieee":"C. P. Goodrich <i>et al.</i>, “Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations,” <i>The Journal of Physical Chemistry B</i>, vol. 111, no. 13. American Chemical Society, pp. 3332–3335, 2007.","chicago":"Goodrich, Carl Peter, Serdal Kirmizialtin, Beatrice M. Huyghues-Despointes, Aiping Zhu, J. Martin Scholtz, Dmitrii E. Makarov, and Liviu Movileanu. “Single-Molecule Electrophoresis of β-Hairpin Peptides by Electrical Recordings and Langevin Dynamics Simulations.” <i>The Journal of Physical Chemistry B</i>. American Chemical Society, 2007. <a href=\"https://doi.org/10.1021/jp071364h\">https://doi.org/10.1021/jp071364h</a>.","apa":"Goodrich, C. P., Kirmizialtin, S., Huyghues-Despointes, B. M., Zhu, A., Scholtz, J. M., Makarov, D. E., &#38; Movileanu, L. (2007). Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. <i>The Journal of Physical Chemistry B</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jp071364h\">https://doi.org/10.1021/jp071364h</a>","ista":"Goodrich CP, Kirmizialtin S, Huyghues-Despointes BM, Zhu A, Scholtz JM, Makarov DE, Movileanu L. 2007. Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. The Journal of Physical Chemistry B. 111(13), 3332–3335.","short":"C.P. Goodrich, S. Kirmizialtin, B.M. Huyghues-Despointes, A. Zhu, J.M. Scholtz, D.E. Makarov, L. Movileanu, The Journal of Physical Chemistry B 111 (2007) 3332–3335.","mla":"Goodrich, Carl Peter, et al. “Single-Molecule Electrophoresis of β-Hairpin Peptides by Electrical Recordings and Langevin Dynamics Simulations.” <i>The Journal of Physical Chemistry B</i>, vol. 111, no. 13, American Chemical Society, 2007, pp. 3332–35, doi:<a href=\"https://doi.org/10.1021/jp071364h\">10.1021/jp071364h</a>.","ama":"Goodrich CP, Kirmizialtin S, Huyghues-Despointes BM, et al. Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. <i>The Journal of Physical Chemistry B</i>. 2007;111(13):3332-3335. doi:<a href=\"https://doi.org/10.1021/jp071364h\">10.1021/jp071364h</a>"},"year":"2007","doi":"10.1021/jp071364h","author":[{"id":"EB352CD2-F68A-11E9-89C5-A432E6697425","full_name":"Goodrich, Carl Peter","orcid":"0000-0002-1307-5074","last_name":"Goodrich","first_name":"Carl Peter"},{"first_name":"Serdal","last_name":"Kirmizialtin","full_name":"Kirmizialtin, Serdal"},{"first_name":"Beatrice M.","last_name":"Huyghues-Despointes","full_name":"Huyghues-Despointes, Beatrice M."},{"full_name":"Zhu, Aiping","last_name":"Zhu","first_name":"Aiping"},{"first_name":"J. Martin","last_name":"Scholtz","full_name":"Scholtz, J. Martin"},{"first_name":"Dmitrii E.","last_name":"Makarov","full_name":"Makarov, Dmitrii E."},{"full_name":"Movileanu, Liviu","first_name":"Liviu","last_name":"Movileanu"}],"extern":"1","article_type":"original","language":[{"iso":"eng"}],"publisher":"American Chemical Society","publication_status":"published","volume":111,"date_published":"2007-03-13T00:00:00Z","status":"public","oa_version":"None","quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2020-04-30T12:19:15Z","intvolume":"       111","abstract":[{"text":"We used single-channel electrical recordings and Langevin molecular dynamics simulations to explore the electrophoretic translocation of various β-hairpin peptides across the staphylococcal α-hemolysin (αHL) protein pore at single-molecule resolution. The β-hairpin peptides, which varied in their folding properties, corresponded to the C terminal residues of the B1 domain of protein G. The translocation time was strongly dependent on the electric force and was correlated with the folding features of the β-hairpin peptides. Highly unfolded peptides entered the pore in an extended conformation, resulting in fast single-file translocation events. In contrast, the translocation of the folded β-hairpin peptides occurred more slowly. In this case, the β-hairpin peptides traversed the αHL pore in a misfolded or fully folded conformation. This study demonstrates that the interaction between a polypeptide and a β-barrel protein pore is dependent on the folding features of the polypeptide. ","lang":"eng"}],"publication":"The Journal of Physical Chemistry B","type":"journal_article"},{"status":"public","quality_controlled":"1","date_created":"2023-08-01T10:37:35Z","abstract":[{"text":"Dynamic self-assembly (DySA) processes occurring outside of thermodynamic equilibrium underlie many forms of adaptive and intellligent behaviors in natural systems. Relatively little, however, is known about the principles that govern DySA and the ways in which it can be extended to artificial ensembles. This article discusses recent advances in both the theory and the practice of nonequilibrium self-assembly. It is argued that a union of ideas from thermodynamics and dynamic systems' theory can provide a general description of DySA. In parallel, heuristic design rules can be used to construct DySA systems of increasing complexities based on a variety of suitable interactions/potentials on length scales from nanoscopic to macroscopic. Applications of these rules to magnetohydrodynamic DySA are also discussed.","lang":"eng"}],"type":"journal_article","keyword":["Materials Chemistry","Surfaces","Coatings and Films","Physical and Theoretical Chemistry"],"title":"Principles and implementations of dissipative (dynamic) self-assembly","month":"01","scopus_import":"1","page":"2482-2496","day":"25","doi":"10.1021/jp054153q","year":"2006","author":[{"last_name":"Fialkowski","first_name":"Marcin","full_name":"Fialkowski, Marcin"},{"full_name":"Bishop, Kyle J. M.","last_name":"Bishop","first_name":"Kyle J. M."},{"last_name":"Klajn","first_name":"Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal"},{"full_name":"Smoukov, Stoyan K.","last_name":"Smoukov","first_name":"Stoyan K."},{"full_name":"Campbell, Christopher J.","last_name":"Campbell","first_name":"Christopher J."},{"full_name":"Grzybowski, Bartosz A.","last_name":"Grzybowski","first_name":"Bartosz A."}],"article_type":"original","publisher":"American Chemical Society","publication_status":"published","volume":110,"date_published":"2006-01-25T00:00:00Z","oa_version":"None","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","intvolume":"       110","publication":"The Journal of Physical Chemistry B","issue":"6","_id":"13430","article_processing_charge":"No","date_updated":"2023-08-08T11:33:08Z","pmid":1,"publication_identifier":{"issn":["1520-6106","1520-5207"]},"citation":{"ieee":"M. Fialkowski, K. J. M. Bishop, R. Klajn, S. K. Smoukov, C. J. Campbell, and B. A. Grzybowski, “Principles and implementations of dissipative (dynamic) self-assembly,” <i>The Journal of Physical Chemistry B</i>, vol. 110, no. 6. American Chemical Society, pp. 2482–2496, 2006.","chicago":"Fialkowski, Marcin, Kyle J. M. Bishop, Rafal Klajn, Stoyan K. Smoukov, Christopher J. Campbell, and Bartosz A. Grzybowski. “Principles and Implementations of Dissipative (Dynamic) Self-Assembly.” <i>The Journal of Physical Chemistry B</i>. American Chemical Society, 2006. <a href=\"https://doi.org/10.1021/jp054153q\">https://doi.org/10.1021/jp054153q</a>.","apa":"Fialkowski, M., Bishop, K. J. M., Klajn, R., Smoukov, S. K., Campbell, C. J., &#38; Grzybowski, B. A. (2006). Principles and implementations of dissipative (dynamic) self-assembly. <i>The Journal of Physical Chemistry B</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jp054153q\">https://doi.org/10.1021/jp054153q</a>","ista":"Fialkowski M, Bishop KJM, Klajn R, Smoukov SK, Campbell CJ, Grzybowski BA. 2006. Principles and implementations of dissipative (dynamic) self-assembly. The Journal of Physical Chemistry B. 110(6), 2482–2496.","short":"M. Fialkowski, K.J.M. Bishop, R. Klajn, S.K. Smoukov, C.J. Campbell, B.A. Grzybowski, The Journal of Physical Chemistry B 110 (2006) 2482–2496.","mla":"Fialkowski, Marcin, et al. “Principles and Implementations of Dissipative (Dynamic) Self-Assembly.” <i>The Journal of Physical Chemistry B</i>, vol. 110, no. 6, American Chemical Society, 2006, pp. 2482–96, doi:<a href=\"https://doi.org/10.1021/jp054153q\">10.1021/jp054153q</a>.","ama":"Fialkowski M, Bishop KJM, Klajn R, Smoukov SK, Campbell CJ, Grzybowski BA. Principles and implementations of dissipative (dynamic) self-assembly. <i>The Journal of Physical Chemistry B</i>. 2006;110(6):2482-2496. doi:<a href=\"https://doi.org/10.1021/jp054153q\">10.1021/jp054153q</a>"},"external_id":{"pmid":["16471845"]},"extern":"1","language":[{"iso":"eng"}]}]