: Electrostatic interactions play a crucial role in protein structure, stability, and function. We present Bluues2, a significantly enhanced web server for calculating electrostatic properties of proteins using the Generalized Born model. The new version features improved accuracy through refined GB radius calculations using NanoShaper for molecular surface generation, extended functionality for analyzing protein-protein and protein-ligand complexes including calculation of binding free energies and electrostatic complementarity, enhanced interface with integrated Mol* structure viewer, and compatibility with the DRMAAtic framework for efficient job management. Bluues2 provides comprehensive electrostatic analyses including pKa predictions, surface potentials, solvation free energies, and complex interface properties in a user-friendly format accessible to both experts and non-specialists.

Bluues2: An enhanced web server for fast and accurate electrostatic analysis of proteins and protein complexes

Piovesan D.;Tosatto S. C. E.
2026

Abstract

: Electrostatic interactions play a crucial role in protein structure, stability, and function. We present Bluues2, a significantly enhanced web server for calculating electrostatic properties of proteins using the Generalized Born model. The new version features improved accuracy through refined GB radius calculations using NanoShaper for molecular surface generation, extended functionality for analyzing protein-protein and protein-ligand complexes including calculation of binding free energies and electrostatic complementarity, enhanced interface with integrated Mol* structure viewer, and compatibility with the DRMAAtic framework for efficient job management. Bluues2 provides comprehensive electrostatic analyses including pKa predictions, surface potentials, solvation free energies, and complex interface properties in a user-friendly format accessible to both experts and non-specialists.
2026
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/3618599
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