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Application of the thermorheologically complex nonlinear Adam-Gibbs model for the glass transition to molecular motion in hydrated proteins.

Authors :
Hodge IM
Source :
Biophysical journal [Biophys J] 2006 Aug 01; Vol. 91 (3), pp. 993-5. Date of Electronic Publication: 2006 May 05.
Publication Year :
2006

Abstract

The nonlinear thermorheologically complex Adam Gibbs (extended "Scherer-Hodge") model for the glass transition is applied to enthalpy relaxation data reported by Sartor, Mayer, and Johari for hydrated methemoglobin. A sensible range in values for the average localized activation energy is obtained (100-200 kJ mol(-1)). The standard deviation in the inferred Gaussian distribution of activation energies, computed from the reported KWW beta-parameter, is approximately 30% of the average, consistent with the suggestion that some relaxation processes in hydrated proteins have exceptionally low activation energies.

Details

Language :
English
ISSN :
0006-3495
Volume :
91
Issue :
3
Database :
MEDLINE
Journal :
Biophysical journal
Publication Type :
Academic Journal
Accession number :
16679368
Full Text :
https://doi.org/10.1529/biophysj.106.080796