Association of proteins in acidic solutions - a case study with beta-globulin.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
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http://ir.cftri.com/2661/
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| Title |
Association of proteins in acidic solutions - a case study with beta-globulin.
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| Creator |
Rajendran, S.
Prakash, V. |
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| Subject |
03 Proteins
01 Oilseeds |
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| 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.
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| Date |
1992
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| Type |
Article
PeerReviewed |
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| Format |
pdf
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| Language |
en
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| 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.. |
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