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Direct observation of hierarchical protein dynamics
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Lewandowski, Józef R., Halse, M. E., Blackledge, Martin and Emsley, Lyndon (2015) Direct observation of hierarchical protein dynamics. Science, 348 (6234). pp. 578-581. doi:10.1126/science.aaa6111
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WRAP_1071602-ch-240815-lewandowski_accepted_manuscript.pdf - Accepted Version - Requires a PDF viewer. Download (5Mb) | Preview |
Official URL: http://dx.doi.org/10.1126/science.aaa6111
Abstract
One of the fundamental challenges of physical biology is to understand the relationship between protein dynamics and function. At physiological temperatures, functional motions arise from the complex interplay of thermal motions of proteins and their environments. Here, we determine the hierarchy in the protein conformational energy landscape that underlies these motions, based on a series of temperature-dependent magic-angle spinning multinuclear nuclear-magnetic-resonance relaxation measurements in a hydrated nanocrystalline protein. The results support strong coupling between protein and solvent dynamics above 160 kelvin, with fast solvent motions, slow protein side-chain motions, and fast protein backbone motions being activated consecutively. Low activation energy, small-amplitude local motions dominate at low temperatures, with larger-amplitude, anisotropic, and functionally relevant motions involving entire peptide units becoming dominant at temperatures above 220 kelvin.
| Item Type: | Journal Article | ||||||||
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| Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
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| Divisions: | Faculty of Science > Chemistry | ||||||||
| Library of Congress Subject Headings (LCSH): | Proteins--Spectroscopic imaging | ||||||||
| Journal or Publication Title: | Science | ||||||||
| Publisher: | American Association for the Advancement of Science | ||||||||
| ISSN: | 0036-8075 | ||||||||
| Official Date: | May 2015 | ||||||||
| Dates: |
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| Volume: | 348 | ||||||||
| Number: | 6234 | ||||||||
| Page Range: | pp. 578-581 | ||||||||
| DOI: | 10.1126/science.aaa6111 | ||||||||
| Status: | Peer Reviewed | ||||||||
| Publication Status: | Published | ||||||||
| Funder: | France. Agence nationale de la recherche (ANR), Seventh Framework Programme (European Commission) (FP7), Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung [Swiss National Science Foundation] (SNSF), European Union International Reintegration Grant (IRG), University of Warwick | ||||||||
| Grant number: | PCV 2007 (ANR), BioNMR 261863 (FP7), 31-132857 (SNSF), PIRG03-GA-2008-231026 (IRG) |
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