Self-association of insulin and the role of hydrophobic bonding: a thermodynamic model of insulin dimerization
β Scribed by Pocker, Y.; Biswas, Subhasis B.
- Book ID
- 126176987
- Publisher
- American Chemical Society
- Year
- 1981
- Tongue
- English
- Weight
- 1009 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-2960
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Synopsis A model has been developed for approximating the free energy of collagen fibril formation (AF,) and the equilibrium solubility of collagen under physiological conditions. The model utilizes an expression of Flory for rodlike polymers, with the modification that the "pure" anisotropic p
The crystal structure of despentapeptide insulin, a monomeric insulin, has been refined at 1.3 A spacing and subsequently used to predict and model the organization in the insulin fibril. The model makes use of the contacts in the densely packed despentapeptide insulin crystal, and takes into accoun