The conformational analysis of substance P analogs using high-field NMR techniques.
High-field nuclear magnetic resonance measurements were carried out on substance P fragments SP4-11' [pGlu5]-SP5-11 and [pGlu6]SP6-11 both at 400 and at 500 MHz. A spectral simulation was carried out on two of these peptides and the coupling constants were interpreted in terms of the conformations. The JNH-CHa coupling constants are all approximately 8 Hz, with the exception of glycine, indicating no preferred conformation for the backbone. For the amino acids other than p-Glu, a comparison of the coupling constant data suggests the same relative rotamer populations for the side chains. Proton longitudinal relaxation time data were measured for all three peptides and support the above conclusions.
Kawaki
H
H
Department of Chemistry, University of Alberta, Edmonton, Canada.
Otter
A
A
Beierbeck
H
H
Kotovych
G
G
Stewart
J M
JM
D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D011487:Protein Conformation; D013373:Substance P / Q000031:analogs & derivatives*
D013373:Substance P