大肠杆菌伴侣蛋白和伴侣素介导的蛋白质折叠与去折叠

Protein folding and unfolding by Escherichia coli chaperones and chaperonins.

作者信息

Gottesman M E, Hendrickson W A

机构信息

Departments of Microbiology and of Biochemistry and Molecular Biophysics, Institute of Cancer Research, Columbia University, New York, NY 10032, USA.

出版信息

Curr Opin Microbiol. 2000 Apr;3(2):197-202. doi: 10.1016/s1369-5274(00)00075-8.

DOI:10.1016/s1369-5274(00)00075-8

PMID:10745003

Abstract

The folding of proteins from their initial unstructured state to their mature form has long been known to be promoted by other proteins known as chaperones and chaperonins. Recent biochemical and structural discoveries have provided dramatic insight into how these folding proteins work. This review will discuss these findings and suggest future experimental directions.

摘要

长期以来，人们一直知道蛋白质从最初的无结构状态折叠成成熟形式是由其他被称为伴侣蛋白和分子伴侣的蛋白质促进的。最近的生化和结构发现为这些折叠蛋白的工作方式提供了深刻的见解。本综述将讨论这些发现，并提出未来的实验方向。