Mechanical unfolding of proteins: insights into biology, structure and folding

被引:82
作者
Forman, Julia R. [1 ]
Clarke, Jane [1 ]
机构
[1] Univ Cambridge, Dept Chem, MRC Ctr Prot Engn, Cambridge CB2 1EW, England
基金
英国惠康基金;
关键词
D O I
10.1016/j.sbi.2007.01.006
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
Since user-friendly atomic force microscopes came onto the market a few years ago, scientists have explored the response of many proteins to applied force. This field has now matured beyond the phenomenological with exciting recent developments, particularly with regards to research into biological questions. For example, detailed mechanistic studies have suggested how mechanically active proteins perform their functions. Also, in vitro forced unfolding has been compared with in vivo protein import and degradation. Additionally, investigations have been carried out that probe the relationship between protein structure and response to applied force, an area that has benefited significantly from synergy between experiments and simulations. Finally, recent technological developments offer exciting new avenues for experimental studies.
引用
收藏
页码:58 / 66
页数:9
相关论文
共 65 条
[1]   Understanding the elasticity of fibronectin fibrils: Unfolding strengths of FN-III and GFP domains measured by single molecule force spectroscopy [J].
Abu-Lail, NI ;
Ohashi, T ;
Clark, RL ;
Erickson, HP ;
Zauscher, S .
MATRIX BIOLOGY, 2006, 25 (03) :175-184
[2]   Complex folding kinetics of a multidomain protein [J].
Batey, S ;
Scott, KA ;
Clarke, J .
BIOPHYSICAL JOURNAL, 2006, 90 (06) :2120-2130
[3]   Cooperative folding in a multi-domain protein [J].
Batey, S ;
Randles, LG ;
Steward, A ;
Clarke, J .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 349 (05) :1045-1059
[4]   Study of the mechanical properties of myomesin proteins using dynamic force spectroscopy [J].
Bertoncini, P ;
Schoenauer, R ;
Agarkova, I ;
Hegner, M ;
Perriard, JC ;
Güntherodt, HJ .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 348 (05) :1127-1137
[5]   Comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein" [J].
Best, RB ;
Hummer, G .
SCIENCE, 2005, 308 (5721)
[6]   Mechanical unfolding of a titin Ig domain: Structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations [J].
Best, RB ;
Fowler, SB ;
Herrera, JLT ;
Steward, A ;
Paci, E ;
Clarke, J .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 330 (04) :867-877
[7]   What can atomic force microscopy tell us about protein folding? [J].
Best, RB ;
Clarke, J .
CHEMICAL COMMUNICATIONS, 2002, (03) :183-192
[8]   A simple method for probing the mechanical unfolding pathway of proteins in detail [J].
Best, RB ;
Fowler, SB ;
Toca-Herrera, JL ;
Clarke, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (19) :12143-12148
[9]   Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation [J].
Best, RB ;
Li, B ;
Steward, A ;
Daggett, V ;
Clarke, J .
BIOPHYSICAL JOURNAL, 2001, 81 (04) :2344-2356
[10]   Chemistry on a single protein, vascular cell adhesion molecule-1, during forced unfolding [J].
Bhasin, N ;
Carl, P ;
Harper, S ;
Feng, G ;
Lu, H ;
Speicher, DW ;
Discher, DE .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (44) :45865-45874