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

被引:0
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作者
Hui Chen [1 ,2 ]
Guangtao Song [2 ]
Yong Zhang [2 ]
Dongchun Ni [3 ]
Xinwei Zhang [2 ]
Yihua Huang [3 ,4 ]
Jizhong Lou [2 ,4 ]
机构
[1] Shenzhen Baoan Women's and Children's Hospital,Jinan University
[2] Key Laboratory of RNA Biology,CAS Center for Excellence in Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences
[3] National Laboratory of Biomacromolecules,CAS Center for Excellence in Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences
[4] University of Chinese Academy of Sciences
基金
中国国家自然科学基金;
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中图分类号
Q617 [生物结构理论];
学科分类号
071011 ;
摘要
Dear Editor.Transmembrane proteins withβ-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 ofβ-strands,ranging from 8-36.To achieve an overall cylindrical topology,the polypeptide chain of aβ-barrel OMP must fold to form a series of anti-parallelβ-strands with eachβ-strand hydrogen-bonding to its neighboring strands (Otzen and Andersen,2013).The folding and insertion of aβ-barrel OMP in vivo requires an evolutionarily conserved multiprotein complex termedβ-barrel assembly machinery(BAM) complex (Noinaj et al.,2015).The structures of the
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页码:334 / 336
页数:3
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