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Postulated effects on water structure of some salts and protein denaturants as inferred from measurements of viscosity B coefficients: Example of HbS polymerization

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Title Postulated effects on water structure of some salts and protein denaturants as inferred from measurements of viscosity B coefficients: Example of HbS polymerization
 
Creator Banerjee, Ramaprasad
FrilIey, Bernard
Guissani, Annie
 
Description 107-117
Viscosity
measurements have been performed on aqueous solutions of some solutes commonly
used in biochemical practice, with a view to determine the B coefficients
and their temperature dependence. The temperature dependence measured for some
anions leads to a ranking of the latter in an order similar to that reported
earlier from entropy data for their postulated efficiency in disrupting
"water structure". The well known dependence of denaturing power of
guanidinium salts on the anions is shown to be related to the temperature
dependence of B coefficients. Urea and formamide do not appear from this criterion
to be significantly "structure- breaking"; alkyl-substituted
derivatives of urea and formamide, on the other hand, possess significant
"structure-forming" properties. The results are of interest in
relation to the known effects of salts and other solutes on the stability of
protein structures in respect of denaturation, subunit dissociation or self assembly.
A typical application is illustrated by studying the effect of two anions,
namely nitrate and sulphate, on the polymerization of sickle cell hemoglobin
(HbS). Nitrate, which is believed to disrupt water structure, acts as an
inhibitor of HbS polymerization which, on the contrary, is favoured by
sulphate, a postulated structure- former.
 
Date 2012-12-31T19:03:52Z
2012-12-31T19:03:52Z
1999-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15423
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.36(2) [April 1999]