HISNAPI

HISNAPI analyzes hotspot residues at nucleic acid–protein interfaces to identify contributors to binding affinity and to characterize their dynamic behavior.

Key Features:

• Hotspot identification: Identifies hotspot residues that significantly contribute to binding affinity and molecular recognition at nucleic acid–protein interfaces.
• Dynamic hot spot analysis: Integrates molecular dynamics simulations to characterize time-dependent behaviors of hotspot residues.
• Free energy and correlation assessment: Applies one-step free energy perturbation to quantify binding-affinity changes and reports intensity and correlation of hotspots with dynamic motions.

Scientific Applications:

• Drug design: Informs design of compounds targeting specific protein–nucleic acid interfaces by characterizing dynamic hotspots and their effects on binding affinity.
• Viral polymerase analysis: Enables analysis of hotspot residues in SARS-CoV-2 RNA-dependent RNA polymerase to support antiviral research.

Methodology:

Integration of molecular dynamics simulations with one-step free energy perturbation to observe residue behavior over time and quantify binding-affinity changes due to mutations or modifications.