Early Nascent Chain Folding Events on the Ribosome

被引：1
|
作者：
Cabrita, Lisa D. [1 ,2 ,3 ]
Dobson, Christopher M. [1 ]
Christodoulou, John [2 ,3 ]
机构：
[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England
[2] Univ London, Birkbeck Coll, London WE1E 6BT, England
[3] UCL, Inst Struct & Mol Biol, London WE1E 6BT, England
来源：
ISRAEL JOURNAL OF CHEMISTRY | 2010年 / 50卷 / 01期
基金：
英国惠康基金; 英国生物技术与生命科学研究理事会;
关键词：
protein folding; ribosome; NMR spectroscopy; structural biology; nascent chain; biosynthesis; PEPTIDYL-TRANSFER-RNA; TRIGGER FACTOR; POLYPEPTIDE-CHAIN; IN-VITRO; EF-G; ESCHERICHIA-COLI; STRUCTURAL BASIS; PROTEIN; TRANSLATION; ELONGATION;
D O I：
10.1002/ijch.201000015
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
To maintain optimal protein homeostasis within the cell, a complex interplay exists between factors determining the production, transport, and folding of nascent chains. Here we review the evidence for the structural and dynamical properties of nascent polypeptide chains as they emerge from the ribosome and that enable them to acquire their biologically active, three-dimensional structures. In particular, we focus on the application of NMR spectroscopy, which is now emerging as a powerful technique to probe the behavior and properties of emerging nascent chains.
引用
收藏
页码：99 / 108
页数：10
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