Protein folding mechanism revealed by single-molecule force spectroscopy experiments
Protein folding mechanism revealed by single-molecule force spectroscopy experiments作者机构：Research Institute for Biomimetics and Soft Matter Fujian Provincial Key Lab for Soft Functional Materials Research Department of Physics Xiamen University Center of Biomedical Physics Wenzhou Institute University of Chinese Academy of Sciences Oujiang Laboratory
出 版 物：《Biophysics Reports》 (生物物理学报(英文))
年 卷 期：2021年第7卷第5期
页 面：399-412页
核心收录：
学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术]
基 金：supported by the National Natural Science Foundation of China (11874309 and11474237) 111 project (B16029) the Start-up grant of Wenzhou Institute,University of Chinese Academy of Sciences(WIUCASQD2021008)
主 题：Protein folding Free energy landscape Force spectroscopy Molten globule state Transition state
摘 要：Force spectroscopy experiments use mechanical force as a control factor to regulate the folding and unfolding process of proteins. Atomic force microscopy has been widely used to study the mechanical stability of proteins, and obtained unfolding forces and unfolding distance of different proteins, while recently, more low force folding and unfolding measurements were done by optical tweezers and magnetic tweezers. Due to the relatively small distortion of the free energy landscape, low force measurements give the free energy landscape information over bigger conformational space. In this review, we summarize the results of force spectroscopy experiments on different proteins. The unfolding distance obtained at high forces by atomic force microscopy are mostly smaller than 2 nm, while the unfolding distances at low forces distribute over a larger range: from a negative value to more than 6 nm. The sizes of the transition states at low force are ～4 nm for most compact two-state globular proteins,which indicates that this transition state might be the general free energy barrier separating the unfolded state and the theoretically predicated molten globule state. Up to now, only a limited number of proteins has been studied at low forces. We expect that more and more proteins with different conformations will be studied at low forces to reveal the general protein folding mechanism.
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