Osmolytes and Protein-Protein Interactions

被引：66

作者：

Rydeen, Amy E. ^{[1
]}

Brustad, Eric M. ^{[1
]}

Pielak, Gary J. ^{[1
,2
,3
,4
]}

机构：

[1] Univ North Carolina Chapel Hill, Dept Chem, Chapel Hill, NC 27599 USA

[2] Univ North Carolina Chapel Hill, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA

[3] Univ North Carolina Chapel Hill, Lineberger Comprehens Canc Ctr, Chapel Hill, NC 27599 USA

[4] Univ North Carolina Chapel Hill, Integrat Program Biol & Genome Sci, Chapel Hill, NC 27599 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2018年 / 140卷 / 24期

基金：

美国国家科学基金会;

关键词：

ESCHERICHIA-COLI; ORGANIC OSMOLYTES; QUINARY STRUCTURE; SELF-ASSOCIATION; OSMOTIC-STRESS; WATER; STABILITY; ACID; MECHANISM; EVOLUTION;

D O I：

10.1021/jacs.8b03903

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Cells survive fluctuations in osmolality by accumulating and depleting highly soluble, usually neutral, small organic compounds. Natural selection has converged on a small set of such molecules, called osmolytes. The biophysical characterization of osmolytes, with respect to proteins, has centered on tertiary structure stability. Data about their effect on protein assemblies, whose formation is driven by surface interactions, is lacking. Here, we investigate the effects of osmolytes and related molecules on the stabilities of a protein and a protein complex. The results demonstrate that osmolytes are not differentiated from other cosolutes by their stabilizing influences on protein tertiary structure but by their compatibility with the interactions between protein surfaces that organize the cellular interior.

引用

页码：7441 / 7444

页数：4

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