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M Vijayan

Publications and source records attributed to M Vijayan.

120 records · Page 7Linked to original sources

X-ray studies on crystalline complexes involving amino acids and peptides. VIII. Head-to-tail arrangement and a specific interaction in the crystal structure of L-arginine acetate.

L-Arginine acetate crystallizes in the monoclinic space group P2(1) with a = 9.229(2), b = 5.178(3), c = 13.271(4) A and beta = 111.4(1) degrees. The crystal structure was solved by direct methods and refined to an R value of 0.058 for 1333 observed reflections. The conformation of the arginine molecules in the crystal is different from those observed in the crystals of L-arginine, its salts and complexes. The crystal structure indicates that complexation with a small carboxylic acid like acetic acid is sufficient to align arginine molecules in a head-to-tail fashion. The structure contains a specific ion-pair interaction, involving electrostatic attraction as well as two nearly parallel, N-H ... O hydrogen bonds, between the guanidyl group and the acetate ion.

Acetates↗

A novel conformation of valinomycin in its barium complex.

Knowledge of the molecular mechanisms involved in ionophore-mediated cation transport would be valuable for understanding many essential functions of biological membranes. Cations are transported in several stages, such as formation of the ionophore-cation complex, diffusion across the cell membrane and subsequent release of the cation. Several conformational rearrangements are involved in this process, and so a detailed understanding of all the conformational possibilities of the ionophore seems to be essential for elucidating the molecular mechanism of ion transport. We are carrying out spectroscopic and crystallographic studies to explore the possible conformational stages of ionophores by complexing them, in different solvents, with cations of various sizes and charges. We report here a novel conformation of the ionophore valinomycin in its barium complex. It can be described as an extended depsipeptide chain, without interval hydrogen bonds, wound in the form of an ellipse with the two barium ions located at the foci.

Barium↗

An analysis of side-chain conformation in proteins.

The crystal structures of a number of globular proteins are currently available. An analysis of the distribution of side-chains among different allowed conformations in these proteins has been carried out. The observed conformations of individual residues are discussed on the basis of well-known stereochemical criteria. The population distribution of side-chains in different allowed regions in conformational space can be explained largely on the basis of simple steric considerations. In addition to examining the conformational behaviour of individual residues, some population distributions of conformational angles of general interest involving groups of residues have also been analyzed.

Amino Acids↗