Entropy calculations on the molten globule state of a protein:: Side-chain entropies of α-lactalbumin

被引：53

作者：

Schäfer, H

Smith, LJ

Mark, AE

van Gunsteren, WF

机构：

[1] ETH Zentrum, Swiss Fed Inst Technol, Chem Phys Lab, CH-8092 Zurich, Switzerland

[2] Univ Oxford, Oxford Ctr Mol Sci, New Chem Lab, Oxford, England

[3] Univ Groningen, Biophys Chem Lab, Groningen, Netherlands

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 2002年 / 46卷 / 02期

关键词：

D O I：

10.1002/prot.1166

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：

We present entropy estimates based on molecular dynamics simulations of models of the molten globule state of the protein a-lactalbumin at low pH. The entropy calculations use the covariance matrix of atom-positional fluctuations and yield the complete configurational entropy. The configurational entropy of the entire protein and of each of its side chains is calculated. Exposed side chains show a larger entropy compared to buried side chains. A comparison to data from rotamer counting is made and significant differences are found. Proteins 2002;46:215-224. (C) 2001 Wiley-Liss, Inc.

引用

页码：215 / 224

页数：10

共 29 条

[1] BIASED PROBABILITY MONTE-CARLO CONFORMATIONAL SEARCHES AND ELECTROSTATIC CALCULATIONS FOR PEPTIDES AND PROTEINS [J].