ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
Thermal confonnalional transformations of globular proteins, chymotrypsinogen, ribo-nudcase and myoglobin in solutions at different pH values were studied microcalorimetrically. It was shown that the heat effects observed in the process of heating have a complicated form and their explanation necessitates an assumption on the existence of two stages of the process separated by temperature: (I) a pre-denaturational stage where the protein partial heat capacity changes are probably connected with a labilization of the globule structure and (II) a denaturational stage representing a single-step transition of the protein into a state with a higher enthalpy. Transitions without enthalpy change, the existence of which is shown for the first time in globular proteins, necessitates a more cautions approach to the thennudynamical analysis of different physical parameters on the basis of the van't Hoff equation.
Additional Material:
14 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.360101009
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