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Heat capacities of globular proteins

✍ Scribed by Yuan, Ye; Wu, Yinhao; Zi, Jian


Book ID
120213954
Publisher
Institute of Physics
Year
2005
Tongue
English
Weight
100 KB
Volume
17
Category
Article
ISSN
0953-8984

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✍ Ge Zhang; Stina Gerdes; Bernhard Wunderlich πŸ“‚ Article πŸ“… 1996 πŸ› John Wiley and Sons 🌐 English βš– 812 KB

## Abstract In an ongoing effort to understand the thermodynamic properties of proteins, solid‐state heat capacities of poly(amino acid)s of all 20 naturally occurring amino acids and 4 copoly(amino acid)s were previously determined using our Advance Thermal Analysis System (ATHAS). Recently, poly(

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The heats of binding of protons m b to three globular proteins, lysozyme, chymotrysinogen A, and oxidized cytochrome c, from pH 11-2 or lower a t 25Β°C were determined by flow microcalorimetry. In addition, the acid-base titrations of cbymotrypsinogen A and oxidized cytochrome c were investigated und