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dc.contributor.authorKISHORE, Nen_US
dc.contributor.authorRANJANAen_US
dc.date.accessioned2011-07-12T20:31:08Zen_US
dc.date.accessioned2011-12-26T12:47:46Zen_US
dc.date.accessioned2011-12-27T05:39:52Z
dc.date.available2011-07-12T20:31:08Zen_US
dc.date.available2011-12-26T12:47:46Zen_US
dc.date.available2011-12-27T05:39:52Z
dc.date.issued2001en_US
dc.identifier.citationJOURNAL OF CHEMICAL THERMODYNAMICS, 33(10), 1325-1344en_US
dc.identifier.issn0021-9614en_US
dc.identifier.urihttp://dx.doi.org/10.1006/jcht.2001.0844en_US
dc.identifier.urihttp://dspace.library.iitb.ac.in/xmlui/handle/10054/3593en_US
dc.identifier.urihttp://hdl.handle.net/10054/3593
dc.description.abstractThe 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.isoenen_US
dc.publisherACADEMIC PRESS LTD ELSEVIER SCIENCE LTDen_US
dc.subjectEgg-White Lysozymeen_US
dc.subjectSecondary Structureen_US
dc.subjectBeta-Lactoglobulinen_US
dc.subjectAlpha-Lactalbuminen_US
dc.subjectFolding Unitsen_US
dc.subjectProteinen_US
dc.subjectTrifluoroethanolen_US
dc.subjectPeptideen_US
dc.subjectAlcoholsen_US
dc.subjectStabilizationen_US
dc.subject.otherRibonuclease Aen_US
dc.subject.otherCytochrome Cen_US
dc.subject.other1,1,1,3,3,3-Hexafluoro-2-Propanolen_US
dc.subject.otherThermal Denaturationen_US
dc.subject.otherDifferential Scanning Calorimetryen_US
dc.subject.otherPreferential Interactionen_US
dc.titleThermodynamics of thermal denaturation of ribonuclease A and cytochrome c in the presence of 1,1,1,3,3,3-hexafluoro-2-propanolen_US
dc.typeArticleen_US


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