Mechanism of the Bell-Shaped Profile of Ribonuclease A activity: Molecular Dynamic Approach

被引：1

作者：

Dayer, Mohammad Reza ^{[1
]}

Ghayour, Omid ^{[2
]}

Dayer, Mohammad Saaid ^{[3
]}

机构：

[1] Shahid Chamran Univ, Dept Biol, Fac Sci, Ahvaz, Iran

[2] Shahid Chamran Univ, Dept Math, Fac Math & Comp Sci, Ahvaz, Iran

[3] Tarbiat Modares Univ, Dept Parasitol & Med Entomol, Tehran, Iran

来源：

PROTEIN JOURNAL | 2012年 / 31卷 / 07期

关键词：

RNase A; Molecular dynamics; Bell shape profile; Salts; Sodium chloride; BOVINE PANCREATIC RIBONUCLEASE; MAGNETIC-RESONANCE; SIMULATION; STABILITY; RNASE; ANGIOGENIN; PATHWAYS; PROTEINS; VALUES; SALT;

D O I：

10.1007/s10930-012-9435-4

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：

Ribonuclease-A is a small enzyme contains an active site with positive charges for its substrate. His(12) and His(119) of its active site play critical role in enzyme catalysis. Salts show a bell-shaped profile on enzyme activity with an optimum salt concentration of about 0.1 M for optimum activity. The mechanism of decreased activity of the enzyme at low salt concentrations is not clear. In this work, we made a new effort to study the molecular events causing inactivation of RNase-A at low concentrations of NaCl. Our molecular dynamic result confirms that decrease in salt concentrations below an optimal level leads to an enzyme structure with lower dynamism and flexibility than that needed for optimum activity.

引用

页码：573 / 579

页数：7

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