Direct test of the Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins

被引:20
作者
Zhou, HX [1 ]
机构
[1] Florida State Univ, Dept Phys, Tallahassee, FL 32306 USA
[2] Florida State Univ, Inst Mol Biophys, Tallahassee, FL 32306 USA
关键词
D O I
10.1021/ja0298491
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The Gaussian-chain model for treating residual charge-charge interactions was critically tested by recent experimental pKa results for individual Asp, Glu, and His residues in the unfolded drkN SH3 domain. Predicted pKa's were in good agreement with experiment. The clustering of Asp and Glu residues along the sequence was suggested to limit pKa shifts and contribute to the folding stability by destabilizing the unfolded state. Copyright © 2003 American Chemical Society.
引用
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页码:2060 / 2061
页数:2
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