PMID: 7544282Aug 1, 1995Paper

Conformation of a tetradecapeptide epitope of myelin basic protein

European Journal of Biochemistry
G L MendzR E Martenson

Abstract

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.

References

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Citations

Dec 10, 1996·Proceedings of the National Academy of Sciences of the United States of America·S J de SouzaW Gilbert
Jun 29, 2004·Micron : the International Research and Review Journal for Microscopy·George HarauzChristophe Farès
May 15, 1997·European Journal of Biochemistry·S Albouz-AboM von Itzstein

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