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.
beta amino acid residues: Conformational characterization of an N- and C-protected homo-beta-(S)-leucine
IACOVINO, Rosa;ISERNIA, Carla;
1997
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.File in questo prodotto:
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