ArticleThe journal of physical chemistry. A2022
Development and Validation of Fluorinated, Aromatic Amino Acid Parameters for Use with the AMBER ff15ipq Protein Force Field.
Article in The journal of physical chemistry. A, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Engineering Protease-Resistant Peptides via Non-Canonical Amino Acids: Design Strategies and Biosynthetic Advances.Bioengineering (Basel, Switzerland) · 2026Review
- Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026Article
- Rational design ofNature communications · 2025Article
- IntegratingJournal of the American Chemical Society · 2024Article
- Fluorinated Protein-Ligand Complexes: A Computational Perspective.The journal of physical chemistry. B · 2024Review
- Integrative approaches for characterizing protein dynamics: NMR, CryoEM, and computer simulations.Current opinion in structural biology · 2024Review
- AMBERff at Scale: Multimillion-Atom Simulations with AMBER Force Fields in NAMD.Journal of chemical information and modeling · 2024Article
- Engineering of enzymes using non-natural amino acids.Bioscience reports · 2022Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
We developed force field parameters for fluorinated, aromatic amino acids enabling molecular dynamics (MD) simulations of fluorinated proteins. These parameters are tailored to the AMBER ff15ipq protein force field and enable the modeling of 4, 5, 6, and 7F-tryptophan, 3F- and 3,5F-tyrosine, and 4F- or 4-CF
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Registered trials
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