Topology of globular proteins. II
β Scribed by Gordon M. Crippen
- Publisher
- Elsevier Science
- Year
- 1975
- Tongue
- English
- Weight
- 321 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0022-5193
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π SIMILAR VOLUMES
## Abstract A series of experiments is suggested to elucidate further the nature of the adsorption of globular proteins on polar solid surfaces. Two ratios of surface energies and the total protein volume are used to characterize the expected form of the adsorbed species. A simple model calculation
## Abstract In an ongoing effort to understand the thermodynamic properties of proteins, solidβstate 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(
The interpretation of A C 3 O (the free energy change for the reaction, globular conformation + randomly coiled conformation, in the absence of denaturant), in terms of the free energies of transfer of various parts of the protein molecule from water to denaturant solution, is unsatisfactory because