An NMR study of the conformations of N-terminal substance P fragments and antagonists.
Three N-terminal fragments of the neurotransmitter Substance P as well as two antagonist heptapeptides containing D-amino-acid residues were studied using different 1D and 2D NMR techniques. Total nonexchangeable 1H-NMR assignments were carried out in D2O and the NH protons were assigned in H2O by means of COSY experiments. The spectral data indicates that there are no preferred conformations for the backbone. The N-terminal tetrapeptide SP1-4-OH exists as a mixture of cis/trans isomers and this effect was studied as a function of pH.
Szöllösy
A
A
Department of Chemistry, University of Alberta, Edmonton, Canada.
Otter
A
A
Stewart
J M
JM
Kotovych
G
G
D000595:Amino Acid Sequence; D007536:Isomerism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011480:Protease Inhibitors; D011487:Protein Conformation; D013373:Substance P
D010446:Peptide Fragments; D011480:Protease Inhibitors; D013373:Substance P