Single-Molecule Force Spectroscopy of Protein Folding

被引：49

作者：

Petrosyan, Rafayel ^{[1
]}

Narayan, Abhishek ^{[1
]}

Woodside, Michael T. ^{[1
]}

机构：

[1] Univ Alberta, Dept Phys, Edmonton, AB T6G 2E1, Canada

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2021年 / 433卷 / 20期

基金：

加拿大自然科学与工程研究理事会;

关键词：

force spectroscopy; protein folding and misfolding; chaperones; co-translational folding; membrane protein folding; MECHANICAL UNFOLDING PATHWAYS; ENERGY-LANDSCAPE; EXPERIMENTAL VALIDATION; MEMBRANE-PROTEINS; ALPHA-SYNUCLEIN; OUTER-MEMBRANE; KINETICS; CHAPERONES; STABILITY; DIFFUSION;

D O I：

10.1016/j.jmb.2021.167207

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 use of force probes to induce unfolding and refolding of single molecules through the application of mechanical tension, known as single-molecule force spectroscopy (SMFS), has proven to be a powerful tool for studying the dynamics of protein folding. Here we provide an overview of what has been learned about protein folding using SMFS, from small, single-domain proteins to large, multi-domain proteins. We highlight the ability of SMFS to measure the energy landscapes underlying folding, to map complex pathways for native and non-native folding, to probe the mechanisms of chaperones that assist with native folding, to elucidate the effects of the ribosome on co-translational folding, and to monitor the folding of membrane proteins. (C) 2021 Elsevier Ltd. All rights reserved.

引用

页数：19

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