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Advances in solid-state relaxation methodology for probing site-specific protein dynamics
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Lewandowski, Józef R. (2013) Advances in solid-state relaxation methodology for probing site-specific protein dynamics. Accounts of Chemical Research, Volume 46 (Number 9). pp. 2018-2027. doi:10.1021/ar300334g ISSN 0001-4842.
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Official URL: http://dx.doi.org/10.1021/ar300334g
Abstract
Dynamics are intimately linked to protein stability and play a crucial role in important biological processes, such as ligand binding, allosteric regulation, protein folding, signaling, and enzymatic catalysis. Solid-state NMR relaxation measurements allow researchers to determine the amplitudes, time scales, and under favorable conditions, directionality of motions at atomic resolution over the entire range of dynamic processes from picoseconds to milliseconds. Because this method allows researchers to examine both the amplitudes and time scales of motions in this range, they can link different tiers of protein motions in protein energy landscapes. As a result, scientists can better understand the relationships between protein motions and functions. Such studies are possible both with the primary targets of solid-state NMR studies, such as amyloid fibrils, membrane proteins, or other heterogeneous systems, and others that researchers typically study by solution NMR and X-ray crystallography. In addition, solid-state NMR, with the absence of tumbling in solution, eliminates the intrinsic size limitation imposed by slow tumbling of large proteins. Thus, this technique allows researchers to characterize interdomain and intermolecular interactions in large complexes at the atomic scale.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
| Journal or Publication Title: | Accounts of Chemical Research | ||||
| Publisher: | American Chemical Society | ||||
| ISSN: | 0001-4842 | ||||
| Official Date: | 26 April 2013 | ||||
| Dates: |
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| Volume: | Volume 46 | ||||
| Number: | Number 9 | ||||
| Page Range: | pp. 2018-2027 | ||||
| DOI: | 10.1021/ar300334g | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access |
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