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Association of proteins in acidic solutions - a case study with beta-globulin.

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Title Association of proteins in acidic solutions - a case study with beta-globulin.
 
Creator Rajendran, S.
Prakash, V.
 
Subject 03 Proteins
01 Oilseeds
 
Description The investigation of the effect of acid pH on the structure of fi-globulin indicated several transitions as a
function of pH. Upon reducing the pH from 7.0, the fl-globulin molecule underwent an expansion due to
hydration up to pH 5.0, and a further increase in H + concentration resulted in unfolding. This' is a single step
cooperative denaturation as indicated by the viscosity profile. At extreme acid pH values (below pH 2.0) the
protein associates or folds to a different conformational motif as shown by blue shift of ultraviolet fluorescence
emission maximum and decrease in reduced viscosity values by more than 30% due to an entropically driven
hydrophobic interaction. The conformational analysis of fl-globulin showed a decrease up to pH 3.0, followed
by an increase in the ordered structure at low pH values indicatin 9 that the low pH values stabilized this new
conformation. These results are discussed in view of the molten globule structure of proteins.
 
Date 1992
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/2661/1/International%20Journal%20of%20Biological%20Macromolecules%2C%20Volume-14%286%20%281992%29%20298-304.pdf
Rajendran, S. and Prakash, V. (1992) Association of proteins in acidic solutions - a case study with beta-globulin. International Journal of Biological Macromolecules, 14 (6). 298-304, 32 ref..