Structural Chemistry

, Volume 7, Issue 2, pp 103–110 | Cite as

Tryptophan-derived peptides. 1: Crystal structure and solution conformation of Boc-Gly-Trp-Ala-OtBu

  • Uffe Anthoni
  • Carsten Christophersen
  • Claus Flensburg
  • Mogens H. Jakobsen
  • Jan Jensen
  • Per H. Nielsen
Article
Received:
Revised:
Accepted:

Abstract

The solid-state structure of Boc-Gly-Trp-Ala-OBut was determined by single-crystal X-ray diffraction analysis. The tripeptide gave crystals belonging to the orthorhombic systemP212121 and at 122.0(5) K:a=11.0663(12),b=14.107(2),c=17.275(2) Å,V=2697.0(5) Å3Z=4,R(F)=0.0259, andRw(F)=0.0695. The peptide adopts a type-Iβ-turn in the solid state with a single, rather weak, intramolecular hydrogen bond between the Boc-CO and Ala-NH groups (N⋯O 3.082(1) Å, <NH⋯O 167(1)°). The conformation of the Boc-Gly-Trp-Ala-OBut peptide has also been studied by1H NMR spectroscopy. The solvent and temperature dependencies of NH chemical shifts suggests that this hydrogen bond is broken and that all amide protons are solvent exposed in CDCl3 and (CD3)2SO.

Key words

Protected tripeptide solution structure crystal structure X-ray analysis NMR analysis 
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Copyright information

© Plenum Publishing Corporation 1996

Authors and Affiliations

  • Uffe Anthoni
    • 1
  • Carsten Christophersen
    • 1
  • Claus Flensburg
    • 2
  • Mogens H. Jakobsen
    • 1
  • Jan Jensen
    • 1
  • Per H. Nielsen
    • 1
  1. 1.Chemical Institute, The H. C. Ørsted InstituteUniversity of CopenhagenCopenhagenDenmark
  2. 2.Centre for Crystallographic Studies, The H. C. Ørsted InstituteUniversity of CopenhagenCopenhagenDenmark

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