Probing the interaction mechanisms between transmembrane peptides and the chaperonin GroEL with fluorescence anisotropy-Reference-Cited by-同舟云学术

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Probing the interaction mechanisms between transmembrane peptides and the chaperonin GroEL with fluorescence anisotropy

Published:2018-04 Issue: Volume:194 Page:1-7
ISSN:1386-1425
Container-title:Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
language:en
Short-container-title:Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy

Author:

Wang Xiaoqiang,Chen Han,Lu Xinwei,Chi Haixia,Li Shixin,Huang Fang

Funder

National Natural Science Foundation of China

China Postdoctoral Science Foundation

Fundamental Research Funds for the Central Universities

Publisher

Elsevier BV

Subject

Spectroscopy,Instrumentation,Atomic and Molecular Physics, and Optics,Analytical Chemistry

Reference48 articles.

1. Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin;Almen;BMC Biol.,2009

2. A comprehensive comparison of transmembrane domains reveals organelle-specific properties;Sharpe;Cell,2010

3. Distinct protein interfaces in transmembrane domains suggest an in vivo folding model;Stevens;Protein Sci.,2004

4. Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane;Castanie-Cornet;BBA-Mol. Cell. Res.,2014

5. Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form;Fei;Proc. Natl. Acad. Sci. U. S. A.,2014

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