Sankar Basu

EnCPdock provides a web tool for analyzing protein-protein interaction complementarity and binding energetics using AI predictions and visualization.

BRANEart evaluates per-residue stability contributions in membrane proteins using specialized statistical potentials, showing agreement with experimental data.

The paper investigates conformational phase transitions in intrinsically disordered proteins using salt-bridge dynamics and statistical physics to reveal self-similar fractal geometries and criticality.

This study develops new energy functions to analyze amino acid interactions in membrane proteins, revealing differences in stability contributions between transmembrane and extramembrane regions.

This study examines the trade-off between electrostatic interactions and structural flexibility in intrinsically disordered proteins by analyzing salt-bridge dynamics in molecular simulations.

The paper introduces CPdock, a new method for protein docking validation using complementarity plots with multi-dielectric electrostatics, showing improved performance on a docking benchmark.

The paper analyzes salt-bridge networks in globular and disordered proteins, highlighting bifurcated salt-bridges as key motifs in protein stabilization and function.

Proteus predicts disorder-to-order transitioning residues in intrinsically disordered proteins using a random forest classifier, outperforming existing methods with higher true positives and precision.