精氨酸
化学
机制(生物学)
蛋白质-蛋白质相互作用
小分子
生物物理学
蛋白质聚集
蛋白质结构
氨基酸
生物化学
生物
物理
量子力学
作者
Tsutomu Arakawa,Yoshiko Kita
出处
期刊:Current Protein & Peptide Science
[Bentham Science Publishers]
日期:2014-08-18
卷期号:15 (6): 608-620
被引量:37
标识
DOI:10.2174/138920371506140818113015
摘要
Arginine is widely used in such applications as protein refolding, solubilization of proteins and small molecules, protein and small molecule formulation, column chromatography and viral inactivation as summarized in this review. What makes arginine effective in these applications is largely based on its ability to suppress protein-protein interactions and protein-surface interactions. The mechanism of these widespread effects of arginine on proteins can be explained at least in part from its unique interactions with the protein surface. Here we describe the modes of the interactions of arginine with model compounds and proteins and also water molecules, and then attempt to explain the mechanism of its effect on proteins by comparing with the interactions that occur between protein and protein denaturants or stabilizers.
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