Conformational lability of two molecular chaperones Hsc70 and gp96: effects of pH and temperature.
作者： Haihong Fan , Ramesh S. Kashi , C. Russell Middaugh
DOI: 10.1016/J.ABB.2006.01.012
关键词: Structure–activity relationship 、 Circular dichroism 、 Lability 、 Protein tertiary structure 、 Protein structure 、 Stereochemistry 、 HSC70 Heat-Shock Proteins 、 Peptide sequence 、 Chemistry 、 Heat shock protein
摘要: Hsc70 and gp96 are two heat shock proteins with molecular chaperone immune-related activities. The dynamic conformational properties of appear to play a critical role in their biological In this study, we investigated the effects pH temperature on states gp96. quaternary, tertiary, secondary structures both evaluated by variety spectroscopic techniques, including far-UV circular dichroism, Trp fluorescence, ANS derivative UV absorption spectroscopy. results summarized compared employing an empirical phase diagram approach. Very similar behaviors seen for despite differences sequence tertiary structure. Both show substantial lability responses changes environment. This study suggests natural selection related functional through common dynamics rather than immediate structural homology.
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