ArticleScientific reports2017
Equilibrium folding dynamics of meACP in water, heavy water, and low concentration of urea.
Article in Scientific reports, 2017. 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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6 citing papers in PubMed, 10 citations in OpenAlex.
- Understanding Isotope Substitution Effects in Water Using the Potential Energy Landscape Formalism for Quantum Liquids.Journal of chemical theory and computation · 2025Article
- Isotope-Substitution Effects on the Thermodynamic, Dynamic, and Structural Properties of Water: HThe journal of physical chemistry. B · 2025Article
- Elucidating the role of water in collagen self-assembly by isotopically modulating collagen hydration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- DThe journal of physical chemistry. B · 2023Review
- Mechanism and quantitative assessment of saturation transfer for water-based detection of the aliphatic protons in carbohydrate polymers.Magnetic resonance in medicine · 2021Article
- Structural Characterization of an ACP fromInternational journal of molecular sciences · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Many proteins fold in apparent two-state behavior, as partially folded intermediates only transiently accumulate and easily escape detection. Besides a native form and a mainly unfolded form, we captured a partially unfolded form of an acyl carrier protein from Micromonospora echinospora (meACP) in the folding/unfolding equilibrium using chemical exchange saturation transfer NMR experiments. The C-terminal region of the partially unfolded form is mainly folded and the N-terminal is unfolded. Furthermore, to understand how the folding process of meACP is influenced by solvent environments, we compared the folding dynamics of meACP in D
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