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P Manavalan

Publications and source records attributed to P Manavalan.

28 records · Page 2Linked to original sources
PubMed1984

Prediction structure type for human leukocyte interferon subtype A from circular dichroism.

Vacuum UV circular dichroism studies were carried out on human leukocyte interferon subtype A. The secondary structure analysis for the CD spectrum shows 59% alpha-helix, 16% antiparallel beta-sheet, no parallel beta-sheet, 18% beta-turns and 13% other structures. The analysis of the CD features for the prediction of tertiary structural class reveals that it is an all-alpha type protein.

Amino Acid Sequence↗
PubMed1981

Conformational energy calculations on enkephalins and enkephalin analogs. Classification of conformations to different configurational types.

Conformational energy calculations were carried out on the peptide enkaphalins (ENK) and selected analogs to find those conformers of low energy. The analogs studied include [D-Ala2]Enk-NH2, [D-Ala2]Enk, [D-Met2, Pro5]Enk-NH2, [D-Ala2, D-Phe5]Enk, [D-Ala2, D-Leu5]Enk, [D-Ala2, (N-Me)Phe4, Met5] Enk-NH2 and [D-Ala2, (N-Me)Met5]Enk-NH2. When the low-energy conformers for all the analogs are compared, different allowed backbone conformations are found which orient the functional side-chains such that three classifications of structures appear. Each classification shows a unique configuration of side-chain positions in space even though different backbone conformations are found within each classification.

Endorphins↗
PubMed1980

Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins.

Amino acid residues acquire characteristic hydrophobic environments in globular proteins. Using the crystal data on 21 proteins, a new scale of hydrophobic indices for the residues is set up. This scale provides valuable information with regard to hydrophobic domains, nucleation sites, surface domains, loop sites and the spatial positions of residues in protein molecules.

Amino Acids↗
PubMed1977

Solvent accessibilities in glycyl, alanyl and seryl dipeptides.

Theoretical studies on glycyl-alanyl and seryl dipeptides were performed to determine the probable backbone and side-group conformations that are preferred for solvent interaction. By following the method of Lee & Richards [(1971) J. Mol. Biol. 55, 379-400], a solute molecule is represented by a set of interlocking spheres of appropriate van der Waals radii assigned to each atom, and a solvent (water) molecule is rolled along the envelope of the van der Waals surface, and the surface accessible to the solvent molecule, and hence the solvent accessibility for a particular conformation of the solute molecule, is computed. From the calculated solvent accessibilities for various conformations, solvation maps for dipeptides were constructed. These solvation maps suggest that the backbone polar atoms could interact with solvent molecules selectively, depending on the backbone conformation. A conformation in the right-handed bridge (zetaR) region is favoured for both solvent interaction and intrachain hydrogen-bonding. Also the backbone side-chain hydrogen-bonding within the same dipeptide fragment in proteins is less favoured than hydrogen-bonding between side chain and water and between side chain and atoms of other residues. Solvent accessibilities suggest that very short distorted alphaR-helical and extended-structural parts may be stabilized via solvent interaction, and this could easily be possible at the surface of the protein molecules, in agreement with protein-crystal data.

Alanine↗