Conformation of a heptadecapeptide comprising the segment encephalitogenic in rhesus monkey.
The 17-residue peptide FKLGGRDSRSGSPMARR derived from myelin basic protein, containing an epitope encephalitogenic in rhesus monkey, has been studied in aqueous solution by high-resolution one- and two-dimensional carbon and proton nuclear magnetic resonance spectroscopy. The resonances of the spectra from both nuclei were assigned with the aid of two-dimensional correlated spectroscopy, pH and solvent titrations, and one-dimensional spin-decoupling techniques and by comparison of the spectra of the heptadecapeptide with those of a phosphorylated form of the peptide, the pentadecapeptide FKLGGRDSRSGSPMA, and the nonapeptide FKLGGRDSR. Amide proton temperature coefficients, coupling constants, 13C- spin-lattice relaxation times, and nuclear Overhauser effect data suggest the existence of three structured regions comprising residues 3-6, 7-12, and 12-14 in the solution conformations of the encephalitogenic heptadecapeptide.
Price
W S
WS
Department of Biochemistry, University of Sydney, NSW, Australia.
Mendz
G L
GL
Martenson
R E
RE
D000595:Amino Acid Sequence; D000818:Animals; D004681:Encephalomyelitis, Autoimmune, Experimental / Q000276:immunology; D000939:Epitopes / Q000276:immunology; D006863:Hydrogen-Ion Concentration; D008253:Macaca mulatta; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000276:immunology; D010446:Peptide Fragments / Q000276:immunology; D010766:Phosphorylation; D011487:Protein Conformation; D011817:Rabbits
D000939:Epitopes; D004676:Myelin Basic Protein; D010446:Peptide Fragments