Nuclear magnetic resonance studies of lysine-vasopressin: structural constraints.
The 220-MHz proton NMR spectra of lysine-vasopressin and some related compounds are examined in deuterated dimethyl sulfoxide to obtain structural information that must be satisfied by any proposed conformation of the molecule. This structural information is in the form of dihedral angles (for rotation about the NH-C(alpha)H bonds) from coupling constants, possible hydrogen bonding of the CONH(2) and backbone amide groups from the temperature-dependence of the chemical shift, and aromatic ring-aromatic ring interaction from the effect of the magnetically anisotropic groups on the chemical shift.
D055598:Chemical Phenomena; D002621:Chemistry; D003903:Deuterium; D007259:Infrared Rays; D007536:Isomerism; D008239:Lysine; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides; D011487:Protein Conformation; D013057:Spectrum Analysis; D013696:Temperature; D014667:Vasopressins
D010455:Peptides; D014667:Vasopressins; D003903:Deuterium; D008239:Lysine