Suppression of the statistical coil state during the α ↔ β transition in homopolypeptides
✍ Scribed by Wayne L. Mattice; Harold A. Scheraga
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1985
- Tongue
- English
- Weight
- 44 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The paragraph following the first paragraph on page 2791 was erroneously dropped in the printing process. It reads as follows:
The lowest-energy packing arrangement for n , = 5 is shown in Fig. 4 with a schematic indication of the pairs of residues that art: in contact.
📜 SIMILAR VOLUMES
## Abstract Monte‐Carlo calculations of geometric and thermodynamic characteristics of the α‐helix and the β‐structure of polypeptides have been carried out. To describe a hydrogen bond both the Lippincott–Schroeder and Morse potentials were used. The internal rotation angles φ and ψ in the α‐helix
## SYNOPSIS Measurements are presented on the time course of chain exchange among two-chain ahelical coiled coils of rabbit tropomyosin. All experiments are in a regime (temperature, protein concentration) in which coiled-coil dimers are the predominant species. Self-exchange in rue-tropomyosin wa
A method is described for preparation of a species of 88 tropomyosin that is sulfhydryl-blocked at C36 and disulfide-cross-linked at C190. Five steps are involved: (1) Rabbit skeletal muscle tropomywin, comprising aa and a8 species, is oxidized with ferricyanide, &sulfide-cross-linking both species