Mechanical unfolding of a β-barrel membrane protein by single-molecule force spectroscopy  

作　　者：Hui Chen Guangtao Song Yong Zhang Dongchun Ni Xinwei Zhang Yihua Huang Jizhong Lou 

机构地区：[1]Shenzhen Baoan Womens and Children's Hospital,Jinan University,Shenzhen 518101,China [2]Key Laboratory of RNA Biology,CAS Center for Excellence in Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences,Beijing 100101,China [3]National Laboratory of Biomacromolecules,CAS Center for Excellence in Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences,Beijing 100101,China [4]University of Chinese Academy of Sciences,Beijing 100084,China

出　　处：《Science China(Life Sciences)》2021年第2期334-336,共3页中国科学（生命科学英文版）

基　　金：supported by the National Basic Research Program of China(2014CB910202);the National Natural Science Foundation of China(11672317,31771015)。

摘　　要：Dear Editor.Transmembrane proteins with β-barrel topology are mainly found in the outer membranes(OMs)of Gram-negative bacteria,mitochondria and chloroplasts(Wimley,2003).These proteins usually contain even numbers of β-strands,ranging from 8-36.To achieve an overall cylindrical topology,the polypeptide chain of a β-barrel OMP must fold to form a series of anti-parallel β-strands with each β-strand hydrogen-bonding to its neighboring strands(Otzen and Andersen,2013).The folding and insertion of a β-barrel OMP in vivo requires an evolutionarily conserved multiprotein complex termedβ-barrel assembly machinery(BAM)complex(Noinaj et al.,2015).

关 键 词：TOPOLOGY CYLINDRICAL BONDING 

分 类 号：Q617[生物学—生物物理学]