[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].
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.
D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011522:Protons; D012996:Solutions; D013057:Spectrum Analysis; D013373:Substance P / Q000031:analogs & derivatives*
D011522:Protons; D012996:Solutions; C052460:substance P, cyclo(H-Glu-Phe-Phe-Gly-Leu-Met-NH(CH2)3-NH-); D013373:Substance P
Opredelenie mezhprotonnykh rasstoianiĭ v peptidakh metodom dvumernoĭ spektroskopii iadernogo éffekta Overkhauzera (NOESY). Konformatsiia tsiklicheskogo analoga "veshchestva P" v rastvore.