Preferred conformation of the terminally blocked (Aib)10 homo-oligopeptide: A long, regular 310-helix
✍ Scribed by Claudio Toniolo; Marco Crisma; Gian Maria Bonora; Ettore Benedetti; Benedetto Dl Blasio; Vincenzo Pavone; Carlo Pedone; Antonello Santini
- Book ID
- 102765831
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1991
- Tongue
- English
- Weight
- 704 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The decapeptidepBrBz-( Aib)lo-OtBu, synthesized by the 5 ( 4 H ) -oxazolone method, crystallizes in the monoclinic space group C2/c with a = 43.901(2), b = 9.289(2), and c = 34.746(3) A; p = 114.69(3) O ; and 2 = 8. The crystals contain one molecule of water associated with each peptide. The structure has been solved by the Patterson method and refined to an R value of 0.073 for 6819 observed reflections. The peptide adopts a regular 310-helical structure stabilized by eight N-H -* -O=C intramolecular 1 + 4 (or Clo) H
bonds. This study has allowed us to characterize this important peptide secondary structure in great detail. The crystal-state conformation agrees well with proposals made on the basis of an ir absorption and 'H-nmr study in solution.