6533b854fe1ef96bd12ae052

RESEARCH PRODUCT

Molecular aggregation in selected crystalline 1:1 complexes of hydrophobicD- andL-amino acids. IV. TheL-phenylalanine series

ÅSmund HusabøArto ValkonenCarl Henrik GörbitzKari Rissanen

subject

chemistry.chemical_classificationMolecular StructureChemistryStereochemistryAminobutyratesPhenylalanineHydrogen BondingStereoisomerismStereoisomerismPhenylalanineGeneral MedicineCrystallography X-RayGeneral Biochemistry Genetics and Molecular BiologyAmino acidValineSide chainIsoleucineLeucineAminobutyratesHydrophobic and Hydrophilic Interactions

description

The amino acid L-phenylalanine has been cocrystallized with D-2-aminobutyric acid, C(9)H(11)NO(2).C(4)H(9)NO(2), D-norvaline, C(9)H(11)NO(2).C(5)H(11)NO(2), and D-methionine, C(9)H(11)NO(2).C(5)H(11)NO(2)S, with linear side chains, as well as with D-leucine, C(9)H(11)NO(2).C(6)H(13)NO(2), D-isoleucine, C(9)H(11)NO(2).C(6)H(13)NO(2), and D-allo-isoleucine, C(9)H(11)NO(2).C(6)H(13)NO(2), with branched side chains. The structures of these 1:1 complexes fall into two classes based on the observed hydrogen-bonding pattern. From a comparison with other L:D complexes involving hydrophobic amino acids and regular racemates, it is shown that the structure-directing properties of phenylalanine closely parallel those of valine and isoleucine but not those of leucine, which shares side-chain branching at C(gamma) with phenylalanine and is normally considered to be the most closely related non-aromatic amino acid.

yearjournalcountryeditionlanguage
2009-04-14Acta Crystallographica Section C Crystal Structure Communications
https://doi.org/10.1107/s0108270109014309