X-ray studies on crystalline complexes involving amino acids and peptides. X. Head-to-tail sequences in the crystal structure of L-lysine acetate.
L-Lysine acetate crystallises in the monoclinic space group P21 with a = 5.411 (1), b = 7.562(1), c = 12.635(2) A and beta = 91.7(1) degrees. The crystal structure was solved by direct methods and refined to an R value of 0.049 using the full matrix least squares method. The conformation and the aggregation of lysine molecules in the structure are similar to those found in the crystal structure of L-lysine L-aspartate. A conspicuous similarity between the crystal structures of L-arginine acetate and L-lysine acetate is that in both cases the strongly basic side chain, although having the largest pK value, interacts with the weakly acidic acetate group leaving the alpha-amino and the alpha-carboxylate groups to take part in head-to-tail sequences. These structures thus indicate that electrostatic effects are strongly modulated by other factors so as to give rise to head-to-tail sequences which have earlier been shown to be an almost universal feature of amino acid aggregation in the solid state.
D000596:Amino Acids; D006860:Hydrogen Bonding; D008239:Lysine; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides; D011487:Protein Conformation; D014961:X-Ray Diffraction
D000596:Amino Acids; D010455:Peptides; D008239:Lysine