Nuclear magnetic resonance spectrum of lysine-vasopressin and its structural implications.
The NMR spectra at 220 MHz of lysinevasopressin and its precursors were measured in dimethyl sulfoxide, and the peaks were assigned to specific protons. Information about hydrogen bonding was obtained from the temperature coefficients of the chemical shifts. With these data, and with several chemical-shift positions and coupling constants, structural information was derived for this polypeptide hormone.
D000595:Amino Acid Sequence; D003903:Deuterium; D004121:Dimethyl Sulfoxide; D008239:Lysine; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000032:analysis; D012996:Solutions; D013696:Temperature; D014667:Vasopressins / Q000032:analysis*
D010455:Peptides; D012996:Solutions; D014667:Vasopressins; D003903:Deuterium; D008239:Lysine; D004121:Dimethyl Sulfoxide