Compressibility gives new insight into protein dynamics and enzyme function

被引:54
作者
Gekko, K [1 ]
机构
[1] Hiroshima Univ, Grad Sch Sci, Dept Math & Life Sci, Higashihiroshima 7398526, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2002年 / 1595卷 / 1-2期
关键词
adiabatic compressibility; amino acid substitution; cavity; enzyme function; ligand binding; protein dynamics;
D O I
10.1016/S0167-4838(01)00358-2
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
The adiabatic compressibility of enzyme is largely influenced by binding of coenzyme and substrate, due to the changes in atomic packing. Amino acid substitution also induces large changes in compressibility parallel to enzyme activity. These results demonstrate that a small alteration of local structure by ligand binding and mutation is dramatically magnified in the flexibility of protein molecule to affect the function. Compressibility gives new insight into protein dynamics and enzyme function from the aspect of atomic packing or cavity which cannot be obtained by other techniques. (C) 2002 Elsevier Science B,V. All rights reserved.
引用
收藏
页码:382 / 386
页数:5
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