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Unfolding pathways of human serum albumin: evidence for sequential unfolding and folding of its three domains

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Title Unfolding pathways of human serum albumin: evidence for sequential unfolding and folding of its three domains
 
Creator SANTRA, MANAS KUMAR
BANERJEE, ABHIJIT
RAHAMAN, OBAIDUR
PANDA, DULAL
 
Subject hsa
pyrene maleimide
npa
gdnhcl
sequential unfolding
 
Description Human serum albumin (HSA) contains three -helical domains (I–III). The unfolding process of these domains was monitored using covalently
bound fluorescence probes; domain I was monitored by N-(1-pyrene)maleimide (PM) conjugated with cys-34, domain II was monitored by the
lone tryptophan residue and domain III was followed by p-nitrophenyl anthranilate (NPA) conjugated with Tyrosine-411 (Tyr-411). Using domain-
specific probes, we found that guanidium hydrochloride-induced unfolding of HSA occurred sequentially. The unfolding of domain II preceded
that of domain I and the unfolding of domain III followed that of domain I. In addition, the domains I and III refolded within the dead time of the
fluorescence recovery experiment while the refolding of domain II occurred slowly. The results suggest that individual domain of a multi-domain
protein can fold and unfold sequentially.
 
Publisher Elsevier
 
Date 2009-04-28T05:27:56Z
2011-12-08T06:48:00Z
2011-12-26T13:01:48Z
2011-12-27T05:46:59Z
2009-04-28T05:27:56Z
2011-12-08T06:48:00Z
2011-12-26T13:01:48Z
2011-12-27T05:46:59Z
2005
 
Type Article
 
Identifier International Journal of Biological Macromolecules 37(4), 200-204
0141-8130
10.1016/j.ijbiomac.2005.10.009
http://hdl.handle.net/10054/1276
http://dspace.library.iitb.ac.in/xmlui/handle/10054/1276
 
Language en