DynMoCo: a Novel AI Framework to Reveal Modular Substructures of Protein From Molecular Dynamics
Mao, L.; Kwak, M.; Ashkezari, A. H. K.; Li, Z.; Chen, Y.; Cong, P.; Phee, J. H.; Kang, S.; Li, J.; Zhu, C.
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Proteins are dynamic molecular machines whose functions are determined by their structures. While static structures can offer initial insights or hypotheses about protein function, they are often insufficient for a detailed mechanistic understanding. Molecular dynamics (MD) simulations provide atomistic view of proteins dynamic motion and conformational change, but the resulting high-dimensional data are challenging to interpret. Traditional summary statistics and dimensionality-reduction methods often focus on global motions and can overlook regional, yet functionally critical motions. Inspired by approaches from social network science, we introduce a novel perspective for analyzing MD simulations through dynamic community detection, where molecules are modeled as time-evolving graphs, and communities of residues or atoms that move coherently or exhibit functional coupling are identified. We present DynMoCo, a novel deep learning framework that integrates graph convolutional networks with recurrent models for end-to-end dynamic community detection on molecular graphs. Given a MD trajectory, DynMoCo identifies spatially grounded substructures, tracks their evolution over time, and can incorporate structural knowledge to ensure physically meaningful communities. We provide a library of custom-written scripts to allow users to extract and visualize these communites on the MD simulated molecules in motion. We demonstrate the method on force-ramp and force-clamp steered MD simulations of three integrin systems, revealing modular substructures within known domains and characterizing their conformational rearrangements during force-induced unbending. By reducing high-dimensional MD data into interpretable communities, this approach offers new insights into the intrinsic organization and dynamic function of complex biomolecular systems. SIGNIFICANCEProteins often perform their functions through dynamic, locally coordinated motions. Molecular dynamics simulations provide detailed views of these motions but produce high-dimensional data that are challenging to analyze and interpret. We present a novel deep learning model that analyzes molecular dynamics simulations data and identifies structurally coherent and potentially functionally related communities, while tracking their temporal evolution. This analysis tool provides a novel way to analyze MD data transforming it into interpretable representations of modular dynamic, enabling discovery of new mechanistic insights and advancing our understanding of how molecular motions drive biological function.
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