消散
耗散系统
分子力学
酶
生物物理学
相(物质)
分子
化学物理
分子动力学
曲面(拓扑)
化学
物理
材料科学
热力学
生物化学
计算化学
量子力学
生物
几何学
数学
作者
Zahra Alavi,Giovanni Zocchi
出处
期刊:Physical review
日期:2018-05-10
卷期号:97 (5)
被引量:2
标识
DOI:10.1103/physreve.97.052402
摘要
Pursuing a materials science approach to understanding the deformability of enzymes, we introduce measurements of the phase of the mechanical response function within the nanorheology paradigm. Driven conformational motion of the enzyme is dissipative as characterized by the phase measurements. The dissipation originates both from the surface hydration layer and the interior of the molecule, probed by examining the effect of point mutations on the mechanics. We also document changes in the mechanics of the enzyme examined, guanylate kinase, upon binding its four substrates. GMP binding stiffens the molecule, ATP and ADP binding softens it, while there is no clear mechanical signature of GDP binding. A hyperactive two-Gly mutant is found to possibly trade specificity for speed. Global deformations of enzymes are shown to be dependent on both hydration layer and polypeptide chain dynamics.
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