ArticleProceedings of the National Academy of Sciences of the United States of America2019
Fast pressure-jump all-atom simulations and experiments reveal site-specific protein dehydration-folding dynamics.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- In silico protein dynamics in the human cytoplasm: Partial folding, misfolding, fold switching, and non-native interactions.Protein science : a publication of the Protein Society · 2023Article
- TMAO: Protecting proteins from feeling the heat.Biophysical journal · 2023Article
- Threading single proteins through pores to compare their energy landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Initiating Coarse-Grained MD Simulations for Membrane-Bound Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Biomolecular Modeling and Simulation: A Prospering Multidisciplinary Field.Annual review of biophysics · 2021Article
- High-pressure small-angle X-ray scattering cell for biological solutions and soft materials.Journal of applied crystallography · 2021Article
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Authors and funding
5 authors.
Funding
Abstract
As theory and experiment have shown, protein dehydration is a major contributor to protein folding. Dehydration upon folding can be characterized directly by all-atom simulations of fast pressure drops, which create desolvated pockets inside the nascent hydrophobic core. Here, we study pressure-drop refolding of three λ-repressor fragment (λ
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