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M Elanthiraiyan

Publications and source records attributed to M Elanthiraiyan.

2 recordsLinked to original sources

Solvent accessibility studies on polysaccharides.

The solvent accessible surface area (ASA) of the polysaccharides, namely (i) carrageenan (1CAR); (ii) agarose (1AGA); (iii) guaran (GUR); (iv) capsular polysaccharide (1CAP); and (v) hyaluronan (1HUA), have been computed using the solvent accessibility technique of Lee and Richards. The results show that the average variation of ASA for the various atoms in the molecules lie in the range 1-30 A(2). Irrespective of position of sulfation, either at two or four in the sugar residues in 1CAR, the charged groups interact almost equally with the solvent. The ASA values for the chains A and B in 1AGA and 1CAR indicate that there are not much interchain interactions and the chains in both the molecules interact equally with the solvent. Residue-wise analysis indicates that the ASAs of residues vary alternately, high-low-high value pattern that is similar to that of the hydrophobic behaviour of beta-strands in proteins. The results also suggest that in these polysaccharides D-configuration residues have higher ASA than L-configuration residues.

Carbohydrate Sequence↗

Solvent accessibility studies on glycosaminoglycans.

Theoretical calculations on the solvent accessible surface area of the commonly occurring glycosaminoglycans (GAGs) have been carried out by employing the solvent accessibility technique of Lee and Richards. The results indicate that the average variation of solvent accessible surface area (ASA) for the different atoms is in the range of 2-28 A2. The average ASA for carbon (9.02 A2) and oxygen (19.3 A2) are relatively very high compared to that for nitrogen and sulfur. The total contribution of ASA by the buried atoms in all the molecules has been found to be small. Heparin complexed with the protein is less accessible to the solvent than the uncomplexed. The iduronic acid is also found to have a varied ASA due to its conformational flexibility. The sulfate groups in heparin have 50% of the total ASA of the molecule. Residue analysis indicates that in general D-configuration residues have higher ASA than L-configuration residues.

Carbohydrate Sequence↗