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mdCATH: A Large-Scale MD Dataset for Data-Driven Computational Biophysics. | LitMetric

mdCATH: A Large-Scale MD Dataset for Data-Driven Computational Biophysics.

ArXiv

Computational Science Laboratory, Universitat Pompeu Fabra, Barcelona Biomedical Research Park (PRBB), Carrer Dr. Aiguader 88, Barcelona, 08003, Spain.

Published: December 2024

AI Article Synopsis

  • Recent advancements in protein structure determination enhance our understanding, but there's a lack of comprehensive datasets on protein dynamics, which are key to protein function.
  • To fill this gap, the authors introduce mdCATH, a dataset created from extensive molecular dynamics simulations of 5,398 protein domains across various temperatures, providing a detailed view of protein behavior.
  • The mdCATH dataset allows for unique statistical analyses of protein unfolding and includes reproducible case studies to demonstrate its potential in advancing protein science.

Article Abstract

Recent advancements in protein structure determination are revolutionizing our understanding of proteins. Still, a significant gap remains in the availability of comprehensive datasets that focus on the dynamics of proteins, which are crucial for understanding protein function, folding, and interactions. To address this critical gap, we introduce mdCATH, a dataset generated through an extensive set of all-atom molecular dynamics simulations of a diverse and representative collection of protein domains. This dataset comprises all-atom systems for 5,398 domains, modeled with a state-of-the-art classical force field, and simulated in five replicates each at five temperatures from 320 K to 450 K. The mdCATH dataset records coordinates and forces every 1 ns, for over 62 ms of accumulated simulation time, effectively capturing the dynamics of the various classes of domains and providing a unique resource for proteome-wide statistical analyses of protein unfolding thermodynamics and kinetics. We outline the dataset structure and showcase its potential through four easily reproducible case studies, highlighting its capabilities in advancing protein science.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11643217PMC

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