可压缩性为蛋白质动力学和酶功能提供了新的见解

Kunihiko Gekko
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引用次数: 59

摘要

酶的绝热压缩性很大程度上受辅酶与底物结合的影响。氨基酸取代也会引起与酶活性相似的压缩性的巨大变化。这些结果表明,配体结合和突变引起的局部结构的微小改变会极大地放大蛋白质分子的柔韧性,从而影响其功能。可压缩性从原子填充或空腔的角度对蛋白质动力学和酶的功能提供了新的认识,这是其他技术无法获得的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Compressibility gives new insight into protein dynamics and enzyme function

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.

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