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Kanagaraj Sekar

Researcher at Indian Institute of Science

Publications -  187
Citations -  2464

Kanagaraj Sekar is an academic researcher from Indian Institute of Science. The author has contributed to research in topics: Protein structure & Protein Data Bank. The author has an hindex of 26, co-authored 181 publications receiving 2205 citations. Previous affiliations of Kanagaraj Sekar include Ohio State University & University of Madras.

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Ramachandran Plot on The Web (2.0)

TL;DR: The Ramachandran plot displays the main chain conformation angles (Phi and Psi) of the polypeptide chain of a protein molecule and has several improved options for displaying the conformation angle in various regions.
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Differential activities of the two closely related withanolides, Withaferin A and Withanone: bioinformatics and experimental evidences.

TL;DR: It is demonstrated that Wi-A that binds strongly to the selected targets acts as a strong cytotoxic agent both for normal and cancer cells, and Wi-N, on the other hand, has a weak binding to the targets; it showed milder cytotoxicity towards cancer cells and was safe for normal cells.
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Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes

TL;DR: The present structure, along with that of the Me-alpha-Gal complex, provides a reasonable qualitative explanation for the known affinities of jacalin to different carbohydrate ligands and a plausible model of the binding of the lectin to T-antigen O-linked to seryl or threonyl residues.
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C-halogen…π interactions in proteins: a database study

TL;DR: In this article, the role of C-X-pi interactions (X = F, Cl, Br, I) in protein structures was investigated and it was shown that the propensity for the formation of C -X-π interactions is higher in case of fluorine than in other halogens.
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Aromatic-aromatic interactions in structures of proteins and protein-DNA complexes: a study based on orientation and distance

TL;DR: This study focuses on the four aromatic amino acid residues and their interactions with one another and their individual interactions with the four nucleotide bases to determine the extent to which their orientation and the number of interactions contribute to the protein and protein-DNA complex structures.