ArticleJournal of chemical theory and computation2015
Empirical Optimization of Interactions between Proteins and Chemical Denaturants in Molecular Simulations.
Article in Journal of chemical theory and computation, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Accuracy of distance distributions and dynamics from single-molecule FRET.Biophysical journal · 2025Article
- Static and Dynamic Correlations in Binary and Ternary Mixtures of TMAO, Urea, and Water.The journal of physical chemistry. B · 2025Article
- The Action of Chemical Denaturants: From Globular to Intrinsically Disordered Proteins.Biology · 2023Review
- Single-molecule Detection of Ultrafast Biomolecular Dynamics with Nanophotonics.Journal of the American Chemical Society · 2022Article
- Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins.Methods (San Diego, Calif.) · 2021Article
- Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Emerging consensus on the collapse of unfolded and intrinsically disordered proteins in water.Current opinion in structural biology · 2020Review
- Evolution of All-Atom Protein Force Fields to Improve Local and Global Properties.The journal of physical chemistry letters · 2019Article
- The combined force field-sampling problem in simulations of disordered amyloid-β peptides.The Journal of chemical physics · 2019Article
- Contrasting Effects of Guanidinium Chloride and Urea on the Activity and Unfolding of Lysozyme.ACS omega · 2018Article
- Inferring properties of disordered chains from FRET transfer efficiencies.The Journal of chemical physics · 2018Article
- Molecular recognition and packing frustration in a helical protein.PLoS computational biology · 2017Article
- Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.Journal of the American Chemical Society · 2016Article
- Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Chemical denaturants are the most commonly used perturbation applied to study protein stability and folding kinetics as well as the properties of unfolded polypeptides. We build on recent work balancing the interactions of proteins and water, and accurate models for the solution properties of urea and guanidinium chloride, to develop a combined force field that is able to capture the strength of interactions between proteins and denaturants. We use solubility data for a model tetraglycine peptide in each denaturant to tune the protein-denaturant interaction by a novel simulation methodology. We validate the results against data for more complex sequences: single-molecule Förster resonance energy transfer data for a 34-residue fragment of the globular protein CspTm and photoinduced electron transfer quenching data for the disordered peptides C(AGQ)nW in denaturant solution as well as the chemical denaturation of the mini-protein Trp cage. The combined force field model should aid our understanding of denaturation mechanisms and the interpretation of experiment.
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