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Insights into the local residual entropy of proteins provided by NMR relaxation
Author(s) -
Li Zhigang,
Raychaudhuri Soumya,
Wand A. Joshua
Publication year - 1996
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560051228
Subject(s) - statistical physics , entropy (arrow of time) , residual , biological system , residual entropy , conformational entropy , relaxation (psychology) , configuration entropy , principle of maximum entropy , physics , chemical physics , chemistry , computational chemistry , thermodynamics , mathematics , molecule , quantum mechanics , biology , algorithm , statistics , neuroscience
A simple model is used to illustrate the relationship between the dynamics measured by NMR relaxation methods and the local residual entropy of proteins. The expected local dynamic behavior of well‐packed extended amino acid side chains are described by employing a one‐dimensional vibrator that encapsulates both the spatial and temporal character of the motion. This model is then related to entropy and to the generalized order parameter of the popular “model‐free” treatment often used in the analysis of NMR relaxation data. Simulations indicate that order parameters observed for the methyl symmetry axes in, for example, human ubiquitin correspond to significant local entropies. These observations have obvious significance for the issue of the physical basis of protein structure, dynamics, and stability.