ArticleBiophysical journal2025
Evaluation and refinement of all-atom force fields for reproducing collagen structure and dynamics.
Article in Biophysical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Free energy of collagen-mimetic peptide dimerization and implications for fibrillization.Biophysical journal · 2026Article
- Collagen as a stress test and a tool for improvement of glycine and proline conformations in biomolecular force fields.Biophysical journal · 2025Article
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Authors and funding
2 authors.
Funding
Abstract
Collagenous protein domains, characterized by the XYGly sequence repeat motif, trimerize and fibrilize to serve as the molecular skeleton of extracellular matrices, and their mutations are frequently associated with disease. Because of experimental challenges in studying the effect of mutations on the properties of collagen, accurate atomistic molecular dynamics simulations are an invaluable tool. We evaluate the accuracy of state-of-the-art molecular dynamics force fields using recent experiments on model peptide homotrimers composed of proline-4(R)-hydroxyproline-glycine (POG) repeats: the stabilizing POG motif appears with high frequency in several types of collagen. POG repeats are used as templates to explore the role of amino acid substitutions in modulating collagen structure. We have compared the structure and dynamics of collagen POG
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Registered trials
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