The mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: Conformational flexibility and molecular chaperone activity-Reference-Cited by-同舟云学术

The mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: Conformational flexibility and molecular chaperone activity

Published:2008-12-31 Issue:1 Volume:8 Page:174-179
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Yang Hongmei,Huang Sufang,Dai Hongzheng,Gong Yandao,Zheng Changxue,Chang Zengyi

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference14 articles.

1. Chaperone-like activity and temperature-induced structural changes of α-crystallin;Bakthisaran;J Biol Chem,1997

2. Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation;Chang;J Biol Chem,1996

3. Mycobacterial stationary phase induced by low oxygen tension: Cell wall thickening and localization of the 16-kilodalton alpha-crystallin homolog;Cunningham;J Bacteriol,1998

4. Detection and characterization of α-crystallin intermediate with maximal chaperone-like activity;Das;Biochem Biophys Res Commn,1997

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