Experimental measurements of disulfide bond stability a t various stages of protein folding are considered in terms of the effective concentrations of the thiol groups relative to each other; values of up to 107M are observed, so that intramolecular interactions within the interior of a protein are
An approach to understanding conformational mobility in peptides and proteins
β Scribed by David L. Turner
- Book ID
- 115781462
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 284 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0006-2952
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Peptides have been an integral part of the collagen tripleβhelix structure story, and have continued to serve as useful models for biophysical studies and for establishing biologically important sequenceβstructureβfunction relationships. High resolution structures of tripleβhelical pept
The energy function of a protein consists of a tremendous number of minima. Locating the global energy minimum (GEM) structure, which corresponds approximately to the native structure, is a severe problem in global optimization. Recently we have proposed a conformational search technique based on th