Tryptophan-derived peptides. 1: Crystal structure and solution conformation of Boc-Gly-Trp-Ala-OtBu |
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| Authors: | Uffe Anthoni Carsten Christophersen Claus Flensburg Mogens H Jakobsen Jan Jensen Per H Nielsen |
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| Institution: | (1) Chemical Institute, The H. C. Ørsted Institute, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark;(2) Centre for Crystallographic Studies, The H. C. Ørsted Institute, University of Copenhagen, Universitetsparken 5, Copenhagen, Denmark |
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| 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, andR
w(F)=0.0695. The peptide adopts a type-I -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, <NHO 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. |
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| Keywords: | Protected tripeptide solution structure crystal structure X-ray analysis NMR analysis |
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