Published April 24, 2023 | Version v1

Phosphorylation at Ser65 modulates ubiquitin conformational dynamics

  • 1. Johns Hopkins University School of Medicine
  • 2. University of California - Irvine

Description

The data deposited here accompany the manuscript "Phosphorylation at Ser65 modulates ubiquitin conformational dynamics" and include molecular dynamics data for equilibrium molecular dynamics simulations, the string method with swarms of trajectories, and metadynamics calculations for ubiquitin and Ser65-phosphorylated ubiquitin systems. We also include the Python code we used to analyze the data for this manuscript. Detailed file contents are summarized in the README files within various subdirectories.  

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analyze_string_and_metadynamics.ipynb

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Additional details

Funding

National Institutes of Health
Program of Molecular Biophysics 1T32GM135131-01