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dc.contributor.authorDeep, Shashank
dc.contributor.authorAhluwalia, J C
dc.date.accessioned2005-12-26T07:17:26Z
dc.date.accessioned2019-02-10T14:24:37Z
dc.date.accessioned2019-02-11T06:17:34Z
dc.date.available2005-12-26T07:17:26Z
dc.date.available2019-02-10T14:24:37Z
dc.date.available2019-02-11T06:17:34Z
dc.date.issued2002
dc.identifier.citationBiophysical Chemistry, 97(1), 73–77en
dc.identifier.urihttp://localhost:8080/iit/handle/2074/1049
dc.description.abstractThe heat capacities (ΔCp,f) for the temperature-induced folding of proteins: barnase, lysozyme T4, papain, trypsin, ribonuclease T1, chymotrypsin, lysozyme and ribonuclease A have been calculated from the change in solvent accessible surface area between the native state and extended polypeptide chain. To visualize the effect of disulfide cross-links on molar heat capacity, loops of varying number of alanine residues and extended alanine chains with terminal cystein are modeled. The difference in ΔCp values between the extended state and the loop conformation of proteins is linearly related to the number of residues in the loop. Corrections to the heat capacity of folding (ΔCp,f) are applied for proteins with cross-links based on this observation. There is good correlation between corrected values of ΔCp,f and experimental values.en
dc.format.extent204049 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoenen
dc.subjectProtein foldingen
dc.subjectProtein stabilityen
dc.subjectHeat capacity of foldingen
dc.subjectSolvent-accessible surface areaen
dc.subjectDisulfide cross-linksen
dc.titleHeat capacity of folding of proteins corrected for disulfide crosslinksen
dc.typeArticleen


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