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Molten globule intermediates of human serum albumin in low concentration of urea

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Title Molten globule intermediates of human serum albumin in low concentration of urea
 
Creator Muralidhara, B K
Prakash, V
 
Description 318-324
Interaction of non-electrolytes such
as urea with proteins especially at lower concentrations is opening-up newer
concepts in the understanding of protein stability and folding in proteomics. In
this study, the secondary and tertiary structural characteristics and thermal
stability of human serum albumin at lower concentrations of urea have been
monitored. The protein attains a molten globule like structure at concentration
urea be low 2M. This structural state also shows an increase in the α-helical
content as compared to the native state. At concentrations of urea above 2M,
human serum albumin starts unfolding, resulting in a three-state transition
with two mid points of transitions at around 4M and 7M urea
concentrations.

The characteristics of the partially
folded intermediates are discussed with respect to the three component system
analyses. Preferential hydration dominates over preferential interaction at
lower concentration of urea (up to 2.5M) and at higher concentration,
the preferential interaction overtakes preferential hydration in a competitive
manner. Formation of structural intermediates at lower concentration of urea is
hypothesized as a general phenomenon in proteins and fits in with the observation
with preferential interaction parameters by Timasheff and co-workers in the
case of Iysozyme and ribonuclease at different pH values.
 
Date 2012-12-08T16:11:39Z
2012-12-08T16:11:39Z
2002-10
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15208
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.39(5) [October 2002]