Study of the CN1 peptide of P2 protein using Fourier transform infra-red spectroscopy.
The conformation of the CN1 peptide, derived from the nervous system P2 protein, has been studied in deuterium oxide solution using Fourier transform infra-red (FTIR) spectroscopy. The peptide was found to be mainly random, with some alpha-helix and beta-structure present. The open structure of CN1 indicates that the constraints necessary for formation of the largely beta-structure in P2 are removed by cleavage of the protein to form peptides. The study produced different quantitative estimations of secondary structures to those previously reported in circular dichroism studies, but the FTIR results are shown to be more reliable.
Stuart
B H
BH
School of Biological and Chemical Sciences, University of Greenwich, London, UK.
McFarlane
E F
EF
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003903:Deuterium; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000737:chemistry*; D018996:Myelin P2 Protein; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
D004676:Myelin Basic Protein; D018996:Myelin P2 Protein; D010446:Peptide Fragments; D003903:Deuterium