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 we...
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Veröffentlicht in: | European journal of biochemistry 1995-08, Vol.231 (3), p.659-666 |
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Sprache: | eng |
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Zusammenfassung: | 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 α‐helix in the N‐terminal segment, and a loop extending from Ser7 to Serl2 that bring His10 and Tyr14 into close proximity. |
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ISSN: | 0014-2956 1432-1033 |
DOI: | 10.1111/j.1432-1033.1995.0659d.x |