Frontofacionasal dysplasia: a new case and review of the phenotype |
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Authors: | W Reardon RM Winter D Taylor M Baraitser |
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Affiliation: | CNRS-UPR 9003, ESBS, Strasbourg, France. |
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Abstract: | The structural features of Arg-Gly-Asp-related sequences have been investigated by 1H and 13C NMR. Two linear peptides which inhibit platelet aggregation with a high efficiency have been studied: D-Arg-Gly-Asp-Trp and L-Arg-Gly-Asp-Trp. Analysis of pH titration effects, amide proton exchange rates and inter-proton distances obtained from ROESY spectra suggest that these small fragments predominantly adopt a type II' beta-turn structure in solution. Folding features of a non-active cyclic peptide based on the same sequence (cyclo-Arg-Gly-Asp-Trp]2) have also been investigated. The biological relevance of these structures is discussed. |
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