Insights into the local residual entropy of proteins provided by NMR relaxation

被引:207
作者
Li, ZG
Raychaudhuri, S
Wand, AJ
机构
[1] SUNY BUFFALO,DEPT CHEM,BUFFALO,NY 14260
[2] SUNY BUFFALO,DEPT BIOL SCI,BUFFALO,NY 14260
[3] SUNY BUFFALO,DEPT BIOPHYS SCI,BUFFALO,NY 14260
[4] SUNY BUFFALO,CTR STRUCT BIOL,BUFFALO,NY 14260
关键词
protein dynamics; protein stability; protein entropy; NMR relaxation;
D O I
10.1002/pro.5560051228
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:2647 / 2650
页数:4
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