Vibrational spectroscopic studies of L,D-alternating phenylalanine peptides.
Infrared and Raman spectra of Boc-(D-Phe-L-Phe)n-OMe, with n = 4 and 5, and Boc-L-Phe-(D-Phe-L-Phe)7-OMe, have been obtained in crystalline and solution states. Based on the earlier spectroscopic studies on Boc-(L-Val-D-Val)n-OMe, with n = 4, 6 and 8, and the predictions from the normal-mode calculations of double-stranded beta-helix conformations, structures have been assigned for the three oligopeptides. In the crystalline state, all three oligopeptides have a double-stranded increases decreases beta 5.6 structure. Spectra from chloroform solution indicate that the solid-state conformation is retained in this solvent for all three oligopeptides.
Naik
V M
VM
Department of Natural Sciences, University of Michigan-Dearborn.
D000595:Amino Acid Sequence; D003460:Crystallization; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012996:Solutions; D013055:Spectrophotometry, Infrared; D013059:Spectrum Analysis, Raman; D013237:Stereoisomerism
D009842:Oligopeptides; D012996:Solutions; D010649:Phenylalanine