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β-Amino acid residues: Conformational characterization of an N- and C-protected homo-β-(S)-leucine

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Abstract

An N- and C-protected derivative of homo-β-leucine, Fmoc-homo-β-(S)-leucine methyl ester, synthesized from the corresponding proteinogenic parent α-amino acid in enantiopure form has been fully characterized in the solid state by X-ray diffraction analysis. The crystal conformation of this new residue indicates an extended conformation for this homo-β-residue, with the ϕ torsion angle being more constrained than the µ and ψ angles.

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Benedetti, E., Iacovino, R., Pedone, C. et al. β-Amino acid residues: Conformational characterization of an N- and C-protected homo-β-(S)-leucine. Letters in Peptide Science 4, 129–134 (1997). https://doi.org/10.1023/A:1008895310236

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  • DOI: https://doi.org/10.1023/A:1008895310236

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