Open AccessCoupled relaxations at the protein–water interface in the picosecond time scale
Author(s) -
Alessandro Paciaroni,
E. Cornicchi,
M. Marconi,
A. Orecchini,
C. Petrillo,
Michael Haertlein,
Martine Moulin,
F. Sacchetti
Publication year - 2009
Publication title -
journal of the royal society interface
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.655
H-Index - 139
eISSN - 1742-5689
pISSN - 1742-5662
DOI - 10.1098/rsif.2009.0182.focus
Subject(s) - picosecond , chemical physics , maltose binding protein , protein dynamics , chemistry , relaxation (psychology) , hydrogen bond , neutron scattering , scale (ratio) , crystallography , scattering , molecular dynamics , physics , molecule , computational chemistry , biology , biochemistry , optics , neuroscience , quantum mechanics , fusion protein , recombinant dna , organic chemistry , laser , gene
The spectral behaviour of a protein and its hydration water has been investigated through neutron scattering. The availability of both hydrogenated and perdeuterated samples of maltose-binding protein (MBP) allowed us to directly measure with great accuracy the signal from the protein and the hydration water alone. Both the spectra of the MBP and its hydration water show two distinct relaxations, a behaviour that is reminiscent of glassy systems. The two components have been described using a phenomenological model that includes two Cole-Davidson functions. In MBP and its hydration water, the two relaxations take place with similar average characteristic times of approximately 10 and 0.2 ps. The common time scales of these relaxations suggest that they may be a preferential route to couple the dynamics of the water hydrogen-bond network around the protein surface with that of protein fluctuations.
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