Thermodynamics of thermal denaturation of ribonuclease A and cytochrome c in the presence of 1,1,1,3,3,3-hexafluoro-2-propanol

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Thermodynamics of thermal denaturation of ribonuclease A and cytochrome c in the presence of 1,1,1,3,3,3-hexafluoro-2-propanol

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dc.contributor.author KISHORE, N en_US
dc.contributor.author RANJANA en_US
dc.date.accessioned 2011-07-12T20:31:08Z en_US
dc.date.accessioned 2011-12-26T12:47:46Z en_US
dc.date.accessioned 2011-12-27T05:39:52Z
dc.date.available 2011-07-12T20:31:08Z en_US
dc.date.available 2011-12-26T12:47:46Z en_US
dc.date.available 2011-12-27T05:39:52Z
dc.date.issued 2001 en_US
dc.identifier.citation JOURNAL OF CHEMICAL THERMODYNAMICS, 33(10), 1325-1344 en_US
dc.identifier.issn 0021-9614 en_US
dc.identifier.uri http://dx.doi.org/10.1006/jcht.2001.0844 en_US
dc.identifier.uri http://dspace.library.iitb.ac.in/xmlui/handle/10054/3593 en_US
dc.identifier.uri http://hdl.handle.net/10054/3593
dc.description.abstract The thermal denaturation of ribonuclease A and cytochrome c has been studied by differential scanning calorimetry (d.s.c.) and u.v.-visible spectrophotometry in the presence of 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) at pH = 5.5 and pH = 4.0, respectively. The quantitative thermodynamic parameters accompanying the thermal transitions from native to denatured state have been evaluated. The results of the reversible thermal denaturations have been fitted with a two-state native-to-denatured mechanism. A comparison has been made of the relative effect of HFIP on the thermal stability of ribonuclease A and cytochrome c. It has been observed that the denaturation capacity of HFIP tends more towards cytochrome c compared with ribonuclease A. The results have been explained on the basis of a fine balance between the preferential exclusion and binding that take place during the course of the denaturation reaction and the structuring of water around the groups of the protein exposed upon denaturation. Using the thermodynamic data obtained from calorimetric and spectroscopic measurements, we have calculated the changes in preferential solvation of ribonuclease A and cytochrome c upon heat denaturation. It is observed that the preferential solvation of these two proteins is specific, indicating that the solvation mechanism is not the same for them. en_US
dc.language.iso en en_US
dc.publisher ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD en_US
dc.subject egg-white lysozyme en_US
dc.subject secondary structure en_US
dc.subject beta-lactoglobulin en_US
dc.subject alpha-lactalbumin en_US
dc.subject folding units en_US
dc.subject protein en_US
dc.subject trifluoroethanol en_US
dc.subject peptide en_US
dc.subject alcohols en_US
dc.subject stabilization en_US
dc.subject.other ribonuclease a en_US
dc.subject.other cytochrome c en_US
dc.subject.other 1,1,1,3,3,3-hexafluoro-2-propanol en_US
dc.subject.other thermal denaturation en_US
dc.subject.other differential scanning calorimetry en_US
dc.subject.other preferential interaction en_US
dc.title Thermodynamics of thermal denaturation of ribonuclease A and cytochrome c in the presence of 1,1,1,3,3,3-hexafluoro-2-propanol en_US
dc.type Article en_US


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