A detailed shape characterization of regular polypeptide conformations
β Scribed by Arteca, Gustavo A.
- Book ID
- 120944602
- Publisher
- NRC Research Press
- Year
- 1995
- Tongue
- French
- Weight
- 566 KB
- Volume
- 73
- Category
- Article
- ISSN
- 0008-4042
- DOI
- 10.1139/v95-033
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π SIMILAR VOLUMES
Inducedjit configurational transitions in proteins can take many forms. In cases, wejind small "closures" of a loop onto the substrate In other cases, the structural changes triggered by a ligand involve large rearrangements that afect entire domains. The nature of these transitions is normally asse
## Abstract AnthopleurinβA (APβA) is a member of a family of sea anemoneβderived polypeptides that interact with sodium channels in a voltageβdependent manner, producing a positive inotropic effect on the mammalian heart. There has been considerable interest in this molecule as a lead compound for
A significant fraction of the socalled ''random coil'' residues in globular proteins exists in the left-handed poly(Pro)II conformation. In order to compare the behavior of this secondary structure with that of the other regular secondary structures, molecular dynamics simulations, with the GROMOS s