The Conformational Analysis of Substance P Analogs Using High-Field NMR Techniques |
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| Authors: | Hideko Kawaki Albin Otter Helmut Beierbeck George Kotovych John M Stewart |
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| Institution: | 1. Department of Chemistry , University of Alberta , Edmonton , Alberta , Canada , T6G 2G2;2. Department of Biochemistry , University of Colorado , Denver , Colorado , 80262 , USA |
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| Abstract: | Abstract 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 ～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. |
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