Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domains  

作　　者：Xueping Li Weili Zhai Zilong Guo Hu Chen 

机构地区：[1]Research Institute for Biomimetics and Soft Matter Fujian Provincial Key Lab for Soft Functional Materials Research Department of Physics,Xiamen University,Xiamen,China

出　　处：《Journal of Innovative Optical Health Sciences》2019年第1期22-28,共7页创新光学健康科学杂志（英文）

基　　金：the National Nature Science Foundation of China(Grant Nos.11474237 and 11574310);the 111 Project(Grant No.B16029).

摘　　要：α-catenin is an adhesion protein located at the cadherin-based cell-cell adherens junction.α-catenin cross-linksβ-catenin and actin fiber in the adhesion protein complex,and plays an important role in the formation and modulation of cell-cell adhesion.The central modulation domains can be unfolded to expose binding site of vinculin when stretching force is applied.Here,we studied the force-induced unfolding dynamics ofα-catenin modulation domains under different loading rates from which the unfolding distance of M2 and M3 domains is determined to be 5-7 nm,and an unfolding intermediate state is identified.We also found that the folding process of M1-M3 domains goes through different pathways with cooperativity.

关 键 词：Α-CATENIN folding and unfolding magnetic tweezer Bell's model 

分 类 号：O313[理学—一般力学与力学基础]