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Multiple-probe analysis of folding and unfolding pathways of human serum albumin - Evidence for a framework mechanism of folding

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Title Multiple-probe analysis of folding and unfolding pathways of human serum albumin - Evidence for a framework mechanism of folding
 
Creator SANTRA, MK
BANERJEE, A
KRISHNAKUMAR, SS
RAHAMAN, O
PANDA, D
 
Subject time-resolved fluorescence
lactalbumin molten globule
small proteins
binding-sites
kinetic role
free-energy
intermediate
state
bilirubin
denaturation
bilirubin
human serum albumin
framework model
nile red
protein folding
 
Description The changes in the far-UV CD signal, intrinsic tryptophan fluorescence and bilirubin absorbance showed that the guanidine hydrochloride (GdnHCl)-induced unfolding of a multidomain protein, human serum albumin (HSA), followed a two-state process. However, using environment sensitive Nile red fluorescence, the unfolding and folding pathways of HSA were found to follow a three-state process and an intermediate was detected in the range 0.25-1.5 m GdnHCl. The intermediate state displayed 45% higher fluorescence intensity than that of the native state. The increase in the Nile red fluorescence was found to be due to an increase in the quantum yield of the HSA-bound Nile red. Low concentrations of GdnHCl neither altered the binding affinity of Nile red to HSA nor induced the aggregation of HSA. In addition, the secondary structure of HSA was not perturbed during the first unfolding transition (
 
Publisher BLACKWELL PUBLISHING LTD
 
Date 2011-07-19T05:40:04Z
2011-12-26T12:51:01Z
2011-12-27T05:37:19Z
2011-07-19T05:40:04Z
2011-12-26T12:51:01Z
2011-12-27T05:37:19Z
2004
 
Type Article
 
Identifier EUROPEAN JOURNAL OF BIOCHEMISTRY, 271(9), 1789-1797
0014-2956
http://dx.doi.org/10.1111/j.1432-1033.2004.04096.x
http://dspace.library.iitb.ac.in/xmlui/handle/10054/5188
http://hdl.handle.net/10054/5188
 
Language en