Document Detail


Protein Surface and Core Dynamics Show Concerted Hydration-Dependent Activation.
MedLine Citation:
PMID:  23154872     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
By specifically labeling leucine/valine methyl groups and lysine side chains "inside" and "outside" dynamics of proteins on the nanosecond timescale are compared using neutron scattering. Surprisingly, both groups display similar dynamics as a function of temperature, and the buried hydrophobic core is sensitive to hydration and undergoes a dynamical transition.
Authors:
Kathleen Wood; François-Xavier Gallat; Renee Otten; Auke J van Heel; Mathilde Lethier; Lambert van Eijck; Martine Moulin; Michael Haertlein; Martin Weik; Frans A A Mulder
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-14
Journal Detail:
Title:  Angewandte Chemie (International ed. in English)     Volume:  -     ISSN:  1521-3773     ISO Abbreviation:  Angew. Chem. Int. Ed. Engl.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370543     Medline TA:  Angew Chem Int Ed Engl     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Affiliation:
Australian Nuclear Science and Technology Organisation Bragg Institute, Menai NSW (Australia); Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, (The Netherlands).
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