Cotranslational protein folding

被引：13

作者：

Kolb, VA ^{[1
]}

机构：

[1] Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia

来源：

MOLECULAR BIOLOGY | 2001年 / 35卷 / 04期

关键词：

D O I：

10.1023/A:1010579111510

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：

The review analyzes the research concerning the folding of proteins in the course of their synthesis on ribosomes. The experimental data obtained for various proteins using various methods give grounds for concluding that a nascent protein largely acquires its spatial structure while still attached to the ribosome, and final foldina into the biologically active conformation takes place as soon as the completed protein is released therefrom. Cotranslational folding is characteristic of both bacterial and eukaryotic cells, and appears to be the universal and the most evolutionarily ancient mechanism.

引用

页码：584 / 590

页数：7

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