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  • Title: [Determination of interproton distances in peptides by two-dimensional nuclear Overhauser effect spectroscopy (NOESY). Conformation of a cyclic analog of substance P in a solution].
    Author: Saulitis IuB, Liepin'sh EE.
    Journal: Bioorg Khim; 1987 Feb; 13(2):168-76. PubMed ID: 2437930.
    Abstract:
    Quantitative method is developed for evaluation interproton distances in peptides in solution. The method is based on the measurement of the relative intensities of the cross-peaks in the pure-phase absorption NOESY spectra. The ratios of the cross-peak intensities IN alpha/I alpha N and INN/I alpha N enable to determine the corresponding interproton distances dN alpha, d alpha N and dNN for several amino acid residues. These distances can be used to estimate other distances with cross-peaks in NOESY spectra. As example, the interproton distances are determined in a cyclic hexapeptide, namely cyclic analogue of substance P: cyclo [H-Glu-Phe-Phe-Gly-Leu-Met-NH(CH2)3-NH-]. The spatial structure of the molecule in dimethylsulphoxide solution is established.
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