The conformation of apamin
β Scribed by C.M. Freeman; C.R.A. Catlow; A.M. Hemmings; R.C. Hider
- Book ID
- 115917967
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 563 KB
- Volume
- 197
- Category
- Article
- ISSN
- 0014-5793
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By replacing two cysteine residues in apamin with selenocysteine, the three possible isomers related to the side-chain connectivities of a bis-cystinyl-peptide were synthesized in regioselective manner exploiting the low redox potential of the diselenide bond. Nuclear magnetic resonance conformation
## Abstract The Xβray structure of [__N__βacetyl]βapamin has been solved at 0.95 Γ resolution. It consists of an 1β7 Nβterminal loop stabilized by an AsnβΞ²βturn motif (2β5 residues) and a helical structure spanning the 9β18 residues tightly linked together by two disulfide bonds. However, neither t