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Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy
The internal motions of integral membrane proteins have largely eluded comprehensive experimental characterization. Here the fast side‐chain dynamics of the α‐helical sensory rhodopsin II and the β‐barrel outer membrane protein W have been investigated in lipid bilayers and detergent micelles by sol...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7318686/ https://www.ncbi.nlm.nih.gov/pubmed/32277554 http://dx.doi.org/10.1002/anie.202003527 |
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author | O'Brien, Evan S. Fuglestad, Brian Lessen, Henry J. Stetz, Matthew A. Lin, Danny W. Marques, Bryan S. Gupta, Kushol Fleming, Karen G. Wand, A. Joshua |
author_facet | O'Brien, Evan S. Fuglestad, Brian Lessen, Henry J. Stetz, Matthew A. Lin, Danny W. Marques, Bryan S. Gupta, Kushol Fleming, Karen G. Wand, A. Joshua |
author_sort | O'Brien, Evan S. |
collection | PubMed |
description | The internal motions of integral membrane proteins have largely eluded comprehensive experimental characterization. Here the fast side‐chain dynamics of the α‐helical sensory rhodopsin II and the β‐barrel outer membrane protein W have been investigated in lipid bilayers and detergent micelles by solution NMR relaxation techniques. Despite their differing topologies, both proteins have a similar distribution of methyl‐bearing side‐chain motion that is largely independent of membrane mimetic. The methyl‐bearing side chains of both proteins are, on average, more dynamic in the ps–ns timescale than any soluble protein characterized to date. Accordingly, both proteins retain an extraordinary residual conformational entropy in the folded state, which provides a counterbalance to the absence of the hydrophobic effect. Furthermore, the high conformational entropy could greatly influence the thermodynamics underlying membrane‐protein functions, including ligand binding, allostery, and signaling. |
format | Online Article Text |
id | pubmed-7318686 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-73186862020-06-29 Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy O'Brien, Evan S. Fuglestad, Brian Lessen, Henry J. Stetz, Matthew A. Lin, Danny W. Marques, Bryan S. Gupta, Kushol Fleming, Karen G. Wand, A. Joshua Angew Chem Int Ed Engl Research Articles The internal motions of integral membrane proteins have largely eluded comprehensive experimental characterization. Here the fast side‐chain dynamics of the α‐helical sensory rhodopsin II and the β‐barrel outer membrane protein W have been investigated in lipid bilayers and detergent micelles by solution NMR relaxation techniques. Despite their differing topologies, both proteins have a similar distribution of methyl‐bearing side‐chain motion that is largely independent of membrane mimetic. The methyl‐bearing side chains of both proteins are, on average, more dynamic in the ps–ns timescale than any soluble protein characterized to date. Accordingly, both proteins retain an extraordinary residual conformational entropy in the folded state, which provides a counterbalance to the absence of the hydrophobic effect. Furthermore, the high conformational entropy could greatly influence the thermodynamics underlying membrane‐protein functions, including ligand binding, allostery, and signaling. John Wiley and Sons Inc. 2020-04-30 2020-06-26 /pmc/articles/PMC7318686/ /pubmed/32277554 http://dx.doi.org/10.1002/anie.202003527 Text en © 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles O'Brien, Evan S. Fuglestad, Brian Lessen, Henry J. Stetz, Matthew A. Lin, Danny W. Marques, Bryan S. Gupta, Kushol Fleming, Karen G. Wand, A. Joshua Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy |
title | Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy |
title_full | Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy |
title_fullStr | Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy |
title_full_unstemmed | Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy |
title_short | Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy |
title_sort | membrane proteins have distinct fast internal motion and residual conformational entropy |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7318686/ https://www.ncbi.nlm.nih.gov/pubmed/32277554 http://dx.doi.org/10.1002/anie.202003527 |
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