X-ray studies on crystalline complexes involving amino acids and peptides. XXXVIII. Crystal structures of the complexes of L-arginine and L-histidine with glutaric acid and a comparative study of amino acid-glutaric acid complexes.
The complexes of glutaric acid with L-arginine and L-histidine (two crystal forms) exhibit different stoichiometries and ionization states. The aggregation patterns in two of the crystals are remarkably similar to those observed earlier in similar structures, while the pattern in the remaining one has not been seen earlier. The variability in the ionization state and stoichiometry observed in amino acid-dicarboxylic acid complexes appears to represent subtle differences in the response of a molecule to the presence in its neighbourhood of another type of molecule. The glutaric acid molecules (or glutarate or semiglutarate ions) in their complexes and in other crystals favour a fully extended conformation, albeit with frequent departures from it. The change in the chirality of the component molecules in the complex could lead to drastic changes in the aggregation pattern; alternatively, the effects of the change are accommodated through small adjustments in essentially the same pattern.
Saraswathi
N T
NT
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
Vijayan
M
M
D000596:Amino Acids / Q000737:chemistry*; D001120:Arginine / Q000737:chemistry; D018360:Crystallography, X-Ray; D005977:Glutarates / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D006860:Hydrogen Bonding; D046911:Macromolecular Substances; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*
D000596:Amino Acids; D005977:Glutarates; D046911:Macromolecular Substances; D010455:Peptides; D006639:Histidine; D001120:Arginine; C035736:glutaric acid