InSty: A ProDy Module for Evaluating Protein Interactions and Stability

ProDy is a widely used application programming interface for analyzing the collective dynamics of proteins and their complexes, offering enhanced capabilities to address the growing needs of the computational biology community to bridge structure and function. Here, we introduce InSty, a new module integrated into ProDy to identify and quantify intra- and intermolecular interactions critical to protein stability and structural dynamics. InSty analyzes the non-covalent interactions using conformational ensemble data from both experiments and computational predictions, assesses their time evolution and persistence during molecular dynamics simulations as well as their conservation across homologs. It provides insights into the significance of these interactions in achieving function and/or supporting stability. InSty outputs lend themselves to statistical evaluation, visualization, and automated ensemble analysis for interpreting the significance of the interactions in the context of protein dynamics, sequence evolution, and allostery. Consolidation of InSty with various ProDy modules enables its efficient usage as a versatile tool that supports mutagenesis studies and identifies critical spots for functional interactions. The InSty module is available as part of the ProDy package at https://github.com/prody/ProDy.

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Publication Details

Journal
Journal of Molecular Biology
Published
2025-02-13
DOI
https://doi.org/10.1016/j.jmb.2025.169009
Citations
4
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
3.22

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article

InSty: A ProDy Module for Evaluating Protein Interactions and Stability

Gary D. Wu, Karolina Mikulska‐Ruminska, Anupam Banerjee, Carlos L. Simmerling et al.
4 citations
Journal of Molecular Biology
Protein Structure and Dynamics
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article

InSty: A ProDy Module for Evaluating Protein Interactions and Stability

Gary D. Wu, Karolina Mikulska‐Ruminska, Anupam Banerjee, Carlos L. Simmerling, Anthony T. Bogetti, Evangelos A. Coutsias, James Krieger, İvet Bahar, Cao Xin, Feng Zhang
article en
4 citations

Abstract

ProDy is a widely used application programming interface for analyzing the collective dynamics of proteins and their complexes, offering enhanced capabilities to address the growing needs of the computational biology community to bridge structure and function. Here, we introduce InSty, a new module integrated into ProDy to identify and quantify intra- and intermolecular interactions critical to protein stability and structural dynamics. InSty analyzes the non-covalent interactions using conformational ensemble data from both experiments and computational predictions, assesses their time evolution and persistence during molecular dynamics simulations as well as their conservation across homologs. It provides insights into the significance of these interactions in achieving function and/or supporting stability. InSty outputs lend themselves to statistical evaluation, visualization, and automated ensemble analysis for interpreting the significance of the interactions in the context of protein dynamics, sequence evolution, and allostery. Consolidation of InSty with various ProDy modules enables its efficient usage as a versatile tool that supports mutagenesis studies and identifies critical spots for functional interactions. The InSty module is available as part of the ProDy package at https://github.com/prody/ProDy.

Journal of Molecular BiologyVol. 437(15)
Nicolaus Copernicus University (PL), Stony Brook School (US), Centro Nacional de Biotecnología (ES), Stony Brook University (US)
European Commission, Narodowe Centrum Nauki, Ministerio de Asuntos Económicos y Transformación Digital, Gobierno de España, National Institutes of Health, Consejo Superior de Investigaciones Científicas
Zero hunger
Openalex Percentile: Top 9%
Protein Structure and Dynamics
3.22
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