| Timescales of Slow Motions in Ubiquitin Explored by Heteronuclear Double Resonance. | |
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MedLine Citation:
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PMID: 22206505 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Understanding how proteins function at the atomic level relies in part on a detailed characterization of their dynamics. Ubiquitin, a small single-domain protein, displays rich dynamic properties over a wide range of timescales. In particular, several regions of ubiquitin show the signature of chemical exchange, including the hydrophobic patch and the β4-α2 loop, which are both involved in many interactions. Here, we use multiple-quantum relaxation techniques to identify the extent of chemical exchange in ubiquitin. We employ our recently developed heteronuclear double resonance method to determine the timescales of motions that give rise to chemical exchange. Dispersion profiles are obtained for the backbone NHN pairs of several residues in the hydrophobic patch and the β4-α2 loop, as well as the C-terminus of helix α1. We show that a single timescale (ca. 50 μs) can be used to fit the data for most residues. Potential mechanisms for the propagation of motions and the possible extent of correlation of these motions are discussed. |
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Authors:
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Nicola Salvi; Simone Ulzega; Fabien Ferrage; Geoffrey Bodenhausen |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-12-28 |
Journal Detail:
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Title: Journal of the American Chemical Society Volume: - ISSN: 1520-5126 ISO Abbreviation: - Publication Date: 2011 Dec |
Date Detail:
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Created Date: 2011-12-30 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7503056 Medline TA: J Am Chem Soc Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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