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Arumay Pal

Researcher at Weizmann Institute of Science

Publications -  18
Citations -  363

Arumay Pal is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Protein structure & DNA. The author has an hindex of 7, co-authored 17 publications receiving 304 citations. Previous affiliations of Arumay Pal include Bose Institute & Agency for Science, Technology and Research.

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The subunit interfaces of weakly associated homodimeric proteins

TL;DR: The weak dimer interfaces may be good models in terms of their size, composition, and evolutionary conservation for the labile subunit contacts that allow protein assemblies to share and exchange components, allosteric proteins to undergo quaternary structure transitions, and molecular machines to operate in the cell.
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ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces

TL;DR: ProFace is a suite of programs that uses a file, containing atomic coordinates of a multi-chain molecule, as input and analyzes the interface between any two or more subunits and can be used to infer if a particular interface belongs to a homodimeric molecule.
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Structure, stability and specificity of the binding of ssDNA and ssRNA with proteins.

TL;DR: A newly developed energy-based coarse-grained model was successfully applied to predict the structure of ssDNA–ssDBP and ssRNA–ssRBP complexes and to assess their sequence-specific interactions and stabilities and tuned two factors that can modulate specific recognition: base–aromatic stacking strength and the flexibility of the single-stranded nucleic acid.
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Peptide segments in protein-protein interfaces.

TL;DR: Dominant segments involved in specific interactions, along with their secondary structural features, are enumerated and can be used as one of the parameters to distinguish between the two types of interfaces.
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Characterization and prediction of the binding site in DNA-binding proteins: improvement of accuracy by combining residue composition, evolutionary conservation and structural parameters

TL;DR: A set of four parameters that in combination can predict DNA-binding residues on protein structures to a high degree of accuracy are presented: number of evolutionary conserved residues and their spatial clustering, hydrogen bond donor capability and residue propensity, and SVM approach for recognizing the interface region.