β-Amino acid residues: Conformational characterization of an N- and C-protected homo-β-(S)-leucine(371 views) Benedetti E, Iacovino R, Pedone C, Rossi F, Saviano M, Isernia C, Montesarchio D, DeNapoli L, Piccialli G
Int J Pept Res Ther (ISSN: 0929-5666, 1573-3149), 1997 Jun; 4(3): 129-134.
Affiliations: Biocrystallography Research Centre, Department of Chemistry, Univ. di Napoli 'Federico II', Via Mezzocannone 4, I-80134 Napels, Italy
Dept. of Organ. and Biol. Chemistry, Univ. di Napoli 'Federico II', Via Mezzocannone 4, I-80134 Napels, Italy
Faculty of Environmental Sciences, II Università di Napoli, Via Arena 22, I-81100 Caserta, Italy
References: Not available.
β-Amino acid residues: Conformational characterization of an N- and C-protected homo-β-(S)-leucine
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.
β-Amino acid residues: Conformational characterization of an N- and C-protected homo-β-(S)-leucine