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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/3593

Title: Thermodynamics of thermal denaturation of ribonuclease A and cytochrome c in the presence of 1,1,1,3,3,3-hexafluoro-2-propanol
Authors: KISHORE, N
RANJANA
Keywords: egg-white lysozyme
secondary structure
beta-lactoglobulin
alpha-lactalbumin
folding units
protein
trifluoroethanol
peptide
alcohols
stabilization
Issue Date: 2001
Publisher: ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
Citation: JOURNAL OF CHEMICAL THERMODYNAMICS, 33(10), 1325-1344
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.
URI: http://dx.doi.org/10.1006/jcht.2001.0844
http://dspace.library.iitb.ac.in/xmlui/handle/10054/3593
http://hdl.handle.net/10054/3593
ISSN: 0021-9614
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