Conformation of a tetradecapeptide epitope of myelin basic protein.
The peptide AcAla-Ser-Gln-Lys-Arg-Pro-Ser-Gln-Arg-His-Gly-Ser-Lys-Tyr, which comprises the first 14 residues of the acetylated N-terminus of myelin basic protein, is an epitopic site for two monoclonal antibodies to the human protein. The conformations of the tetradecapeptide in aqueous solutions were investigated employing high-resolution 1H- and 13C-NMR spectroscopy. Two-dimensional techniques were used to assign the spectra observed from both nuclei. Nuclear-Overhauser-effect data, amide proton temperature coefficients, 13C spin-lattice relaxation times, distance geometry calculations and dynamic simulated annealing provided evidence that the solution conformations of the tetradecapeptide included a nascent alpha-helix in the N-terminal segment, and a loop extending from Ser7 to Ser12 that bring His10 and Tyr14 into close proximity.
Mendz
G L
GL
School of Biochemistry and Molecular Genetics, University of New South Wales, Sydney, Australia.
Barden
J A
JA
Martenson
R E
RE
D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D000939:Epitopes / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000737:chemistry* / Q000276:immunology; D011487:Protein Conformation; D011817:Rabbits
D002247:Carbon Isotopes; D000939:Epitopes; D004676:Myelin Basic Protein