The solution structure of [Ala4]-desdimethylchlamydocin: a 1H n.m.r. relaxation study
- 1 January 1985
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Perkin Transactions 1
- No. 2,p. 245-250
- https://doi.org/10.1039/p19850000245
Abstract
Many fungal peptides exhibit plant toxicity in a host-specific manner. Here we report a proton relaxation and two dimensional (2D) n.m.r. study of the [Ala4]-desdimethyl analogue of the fungal tetrapeptide chlamydocin. Interproton distances calculated from n.m.r. parameters agreed substantially with the corresponding distances in the crystalline form of dihydrochlamydocin. A solution conformational analysis was performed based on n.m.r. distance measurements and φ, ψ, and ω angles of the four residues plus χi rotamer populations. These data support the use of proton relaxation parameters as a basis for accurate solution conformational analysis. As a corollary, the data can also indicate within experimental error that the crystal and solution conformations of chlamydocin and the [Ala4]-desdimethyl analogue, respectively, are identical.This publication has 10 references indexed in Scilit:
- The backbone and side chain conformations of the cyclic tetrapeptide HC-toxinBiochemical and Biophysical Research Communications, 1983
- The structure and conformation of HC-toxinBiochemical and Biophysical Research Communications, 1983
- Nuclear Overhauser effect and cross-relaxation rate determinations of dihedral and transannular interproton distances in the decapeptide tyrocidine ABiophysical Journal, 1980
- Study of the stereochemistry, relaxation mechanisms, and internal motions of natural products utilizing proton relaxation parameters: solution and crystal structures of saxitoxinJournal of the American Chemical Society, 1980
- Observation of 3 .fwdarw. 1 intramolecular hydrogen bonds (.gamma. turns) in the cyclic tetrapeptides, [Ala4]-desdimethylchlamydocin and cyclo-(D-Phe-Pro-D-Phe-Pro), by NMR spectrometry. Effect of solvent on solution conformationJournal of the American Chemical Society, 1980
- Determination of individual side-chain conformations, tertiary conformations, and molecular topography of tyrocidine A from scalar coupling constants and chemical shiftsBiochemistry, 1979
- The quantitation of nuclear Overhauser effect methods for total conformational analysis of peptides in solution. Application to gramicidin SBiophysical Journal, 1978
- Analysis of the 1H‐NMR spectra of ferrichrome peptides. II. The amide resonancesBiopolymers, 1978
- Conformational and ion binding studies of a cyclic pentapeptide. Evidence for .beta. and .gamma. turns in solutionJournal of the American Chemical Society, 1978
- Intramolecular proton nuclear Overhauser effect study of the solution conformation of valinomycin in dimethyl sulfoxideBiochemistry, 1976