Nonadditive effects of mixed crowding on protein stability

被引：85

作者：

Batra, Jyotica

Xu, Ke

Zhou, Huan-Xiang ^{[1
]}

机构：

[1] Florida State Univ, Dept Phys, Tallahassee, FL 32306 USA

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2009年 / 77卷 / 01期

关键词：

protein stability; protein folding; macromolecular crowding; mixed crowding; FKBP; ALPHA-CHYMOTRYPSIN; FREE-ENERGY; IN-VIVO; DENATURATION; DEXTRAN; BINDING; SALT; PH;

D O I：

10.1002/prot.22425

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

The crowded environments inside cells can have significant effects on the folding stability and other biophysical properties of proteins. In this study on how macromolecular crowding affects protein folding, we took a significant step toward realistically mimicking intracellular environments by using a mixture of two crowding agents, Ficoll and dextran. We found that the mixed crowding exerts a greater stabilizing effect than the sum of the two individual crowding agents. Therefore, the composition of crowders, not just the total concentration, has a significant influence on the effects of crowding on protein folding. Since the composition of intracellular macromolecules varies within the lifetime of a cell, our finding may provide an explanation for age being an important risk factor for protein aggregation-related diseases such as Alzheimer's disease. ease and Parkinson disease.

引用

页码：133 / 138

页数：6

共 23 条

[1]

15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions [J].