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Protein Surface and Core Dynamics Show Concerted Hydration‐Dependent Activation
Author(s) -
Wood Kathleen,
Gallat FrançoisXavier,
Otten Renee,
van Heel Auke J.,
Lethier Mathilde,
van Eijck Lambert,
Moulin Martine,
Haertlein Michael,
Weik Martin,
Mulder Frans A. A.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201205898
Subject(s) - protein dynamics , chemical physics , dynamics (music) , valine , chemistry , molecular dynamics , core (optical fiber) , nanosecond , neutron scattering , side chain , crystallography , biophysics , scattering , methyl group , surface protein , leucine , physics , computational chemistry , group (periodic table) , amino acid , biochemistry , biology , organic chemistry , optics , laser , polymer , acoustics , virology
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 (see picture). 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.