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Intermolecular interactions and protein dynamics by solid-state NMR spectroscopy
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Lamley, Jonathan M., Öster, Carl, Stevens, Rebecca A. and Lewandowski, Józef R. (2015) Intermolecular interactions and protein dynamics by solid-state NMR spectroscopy. Angewandte Chemie International Edition, 54 (51). pp. 15374-15378. doi:10.1002/anie.201509168 ISSN 1433-7851.
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Official URL: http://dx.doi.org/10.1002/anie.201509168
Abstract
Understanding the dynamics of interacting proteins is a crucial step toward describing many biophysical processes. Here we investigate the backbone dynamics for protein GB1 in two different assemblies: crystalline GB1 and the precipitated GB1–antibody complex with a molecular weight of more than 300 kDa. We perform these measurements on samples containing as little as eight nanomoles of GB1. From measurements of site-specific 15N relaxation rates including relaxation dispersion we obtain snapshots of dynamics spanning nine orders of magnitude in terms of the time scale. A comparison of measurements for GB1 in either environment reveals that while many of the dynamic features of the protein are conserved between them (in particular for the fast picosecond–nanosecond motions), much greater differences occur for slow motions with motions in the >500 ns range being more prevalent in the complex. The data suggest that GB1 can potentially undergo a small-amplitude overall anisotropic motion sampling the interaction interface in the complex.
| Item Type: | Journal Article | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QP Physiology | ||||||||
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||||||
| Library of Congress Subject Headings (LCSH): | Proteins -- Analysis, Nuclear magnetic resonance spectroscopy, Biophysics | ||||||||
| Journal or Publication Title: | Angewandte Chemie International Edition | ||||||||
| Publisher: | Wiley | ||||||||
| ISSN: | 1433-7851 | ||||||||
| Official Date: | 2 November 2015 | ||||||||
| Dates: |
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| Volume: | 54 | ||||||||
| Number: | 51 | ||||||||
| Page Range: | pp. 15374-15378 | ||||||||
| DOI: | 10.1002/anie.201509168 | ||||||||
| Status: | Peer Reviewed | ||||||||
| Publication Status: | Published | ||||||||
| Access rights to Published version: | Open Access (Creative Commons) | ||||||||
| Date of first compliant deposit: | 31 December 2015 | ||||||||
| Date of first compliant Open Access: | 31 December 2015 | ||||||||
| Funder: | European Research Council (ERC), European Union (EU), Royal Society (Great Britain), Engineering and Physical Sciences Research Council (EPSRC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) | ||||||||
| Grant number: | ERC 639907, RG130022, EP/L025906/1, BB/L022761/1, 316630 | ||||||||
| Is Part Of: | European Research Council European Union. Grant Number: 639907 Royal Society. Grant Number: RG130022 EPSRC. Grant Number: EP/L025906/1 BBSRC. Grant Number: BB/L022761/1 European Union. Grant Number: 316630 EPSRC BBSRC. Grant Number: PR140003 AWM ERDF NIGMS. Grant Number: P41-GM103311 |
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