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• W2085546856 abstract "We have synthesized by solution methods and fully characterized the Nα-blocked heptapeptide methylamide mBrBz-[L-Iva-L-(αMe)Val]2-L-(αMe)Phe-L-(αMe)Val-L-Iva-NHMe, fully based on conformationally constrained Cα-methylated α-amino acids. An X-ray diffraction investigation of the Nα-benzyloxycarbonylated analogue showed that in the crystal state both independent molecules (A and B) in the asymmetric unit of the peptide adopt a fully developed, regular, right-handed 310-helical structure, although molecule A would be slightly distorted at the C-terminal residue. Solution conformational analysis on the mBrBz-blocked peptide was carried out in CDCl3 by means of NMR spectroscopy. For structure determination we performed restrained molecular dynamics simulations in CDCl3 based on a search of the conformational space derived from a simulated annealing strategy. For this peptide the NMR observables can be described by a single backbone conformation, more specifically a rigid 310-helix spanning the amino acid sequence from residue 1 to residue 6. The C-terminal methylamido NH group seems to be involved simultaneously in two H-bonds (with the preceding i − 3 and i − 4 carbonyl groups). Although in this peptide model there are no distinct NOE distances for discriminating 310- versus α-helix conformation, the sum of all NMR-derived restraints clearly results in a 310-helical structure. Convergence from different starting structures (including an α-helix) into a 310-helix was observed." @default.
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• W2085546856 date "1998-05-01" @default.
• W2085546856 modified "2023-10-16" @default.
• W2085546856 title "First Step Toward the Quantitative Identification of Peptide 3₁₀-Helix Conformation with NMR Spectroscopy: NMR and X-ray Diffraction Structural Analysis of a Fully-Developed 3₁₀-Helical Peptide Standard" @default.
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• W2085546856 doi "https://doi.org/10.1021/ja9731478" @default.
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