The Power of Force: Insights into the Protein Folding Process Using Single-Molecule Force Spectroscopy

被引:21
作者
Schonfelder, Jorg [1 ]
De Sancho, David [1 ,2 ]
Perez-Jimenez, Raul [1 ,2 ]
机构
[1] CIC nanoGUNE, Tolosa Hibilbidea 76, San Sebastian 20018, Spain
[2] Ikerbasque, Basque Fdn Sci, Bilbao 48013, Spain
关键词
single-molecule; protein folding; force spectroscopy; UNFOLDING PATHWAYS; CONFORMATIONAL DYNAMICS; MECHANICAL STABILITY; FLUCTUATION THEOREM; CLAMP SPECTROSCOPY; ENERGY LANDSCAPES; OPTICAL TWEEZERS; SLOW DIFFUSION; TRANSITION; TITIN;
D O I
10.1016/j.jmb.2016.09.006
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
One of the major challenges in modern biophysics is observing and understanding conformational changes during complex molecular processes, from the fundamental protein folding to the function of molecular machines. Single-molecule techniques have been one of the major driving forces of the huge progress attained in the last few years. Recent advances in resolution of the experimental setups, aided by theoretical developments and molecular dynamics simulations, have revealed a much higher degree of complexity inside these molecular processes than previously reported using traditional ensemble measurements. This review sums up the evolution of these developments and gives an outlook on prospective discoveries. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:4245 / 4257
页数:13
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