SUBSTRATE BINDING SITE FLEXIBILITY OF SMALL HEAT SHOCK PROTEINS AND FACTORS CONTRIBUTING TO EFFICIENT CHAPERONE ACTIVITY

SUBSTRATE BINDING SITE FLEXIBILITY OF SMALL HEAT SHOCK PROTEINS AND FACTORS CONTRIBUTING TO EFFICIENT CHAPERONE ACTIVITY

sHSPs maintain partially denaturing substrates in a soluble sHSP-substrate complex. The heterogeneous interaction between sHSPs and substrate within the complex has prevented a detailed study of the mechanism of sHSP substrate protection. Here, purified sHSPs and heat sensitive substrates were used...

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Bibliographic Details
Main Author: Jaya, Nomalie Naomi
Other Authors: Vierling, Elizabeth
Language:EN
Published: The University of Arizona. 2009
Subjects:
Alpha-crystallin
Chaperones
Cross-linking
Intrinsic disorder
Mass spectrometry
Protein-protein interactions
Online Access:http://hdl.handle.net/10150/193550

Internet

http://hdl.handle.net/10150/193550

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