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Structural perturbation of proteins in low denaturant concentrations

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Title Structural perturbation of proteins in low denaturant concentrations
 
Creator Basak, Soumen
Debnath, Dilip
Haque, Emdadul
Ray, Sibnath
Chakrabarti, Abhijit
 
Description 84-89
The presence of very low concentrations
of the widely used chemical denaturants, guanidinium chloride and urea, induce
changes in the tertiary structure of proteins. We have presented results on
such changes in four structurally unrelated proteins to show that such
structural perturbations are common irrespective of their origin. Data
representative of such

structural changes are shown for the monomeric
globular proteins such as horseradish peroxidase (HRP) from a plant, human serum
albumin (HSA) and prothrombin from ovine blood serum and for the
membrane-associated, worm-like elongated protein, spectrum from ovine
erythrocytes. Structural alterations in these proteins were reflected in quenching

studies of tryptophan fluorescence using
the widely used quencher acrylamide. Stern-Volmer quenching constants measured
in presence of the denaturants, even at concentrations below 100 mM, were
higher than those measured in absence of the de naturants. Both steady-state
and time-resolved fluorescence emission properties of tryptophan and of the
extrinsic probe

PRODAN were used for monitoring
conformational changes in the proteins in presence of different low
concentrations of the denaturants. These results are consistent with earlier
studies from our laboratory indicating structural perturbations in proteins at
the tertiary level, keeping their native-like secondary structure and their
biological activity more or less intact.
 
Date 2013-07-16T06:13:03Z
2013-07-16T06:13:03Z
2001-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/19804
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.38(1-2) [February-April 2001]