Conformational analysis of apamin using the residual representation
β Scribed by Bernard Busetta
- Book ID
- 115910673
- Publisher
- Elsevier Science
- Year
- 1980
- Tongue
- English
- Weight
- 455 KB
- Volume
- 112
- 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