ArticleProceedings of the National Academy of Sciences of the United States of America2016
How the hydrophobic factor drives protein folding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 100 citations in OpenAlex.
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- Differences and Similarities in Protein and Nucleic Acid Structures and Their Biological Interactions.Current issues in molecular biology · 2025Review
- The Arch from the Stones: Understanding Protein Folding Energy Landscapes via Bioinspired Collective Variables.The journal of physical chemistry letters · 2025Article
- Network Dynamics as Fingerprints of Thermostability in an In Silico-Engineered DyP-Type Peroxidase.ACS catalysis · 2025Article
- Exploring the temperature dependence of β-hairpin peptide self-assembly.Faraday discussions · 2025Article
- Could Hydrophobicity of Sulfated Pseudo-Trisaccharides Derived from Repurposing Aminoglycoside Tobramycin Modulate the Enzymatic Activity of Heparanase?Journal of medicinal chemistry · 2025Article
- Problematic Attributions of Entropic and Hydrophobic Effects in Drug Interactions.ACS bio & med chem Au · 2025Review
- Enhancing the Thermostability ofMolecules (Basel, Switzerland) · 2025Article
- Beta Sandwich-Like Folds: Sequences, Contacts, Classification of Invariant Substructures and Beta Sandwich Protein Grammar.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Molecular Insight into the Processes and Mechanisms of NMolecules (Basel, Switzerland) · 2024Article
- Free Energy Density of a Fluid and Its Role in Solvation and Binding.Journal of chemical theory and computation · 2024Article
- Structure and dynamics of liquid water fromChemical science · 2024Article
- A Tale of Two Chains: Geometries of a Chain Model and Protein Native State Structures.Polymers · 2024Article
- The temperature-dependence of host-guest binding thermodynamics: experimental and simulation studies.Chemical science · 2023Article
- Ordered-domain unfolding of thermophilic isolated β subunit ATP synthase.Protein science : a publication of the Protein Society · 2023Article
- Inferring Pathways of Oxidative Folding from Prefolding Free Energy Landscapes of Disulfide-Rich Toxins.The journal of physical chemistry. B · 2023Article
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2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
How hydrophobicity (HY) drives protein folding is studied. The 1971 Nozaki-Tanford method of measuring HY is modified to use gases as solutes, not crystals, and this makes the method easy to use. Alkanes are found to be much more hydrophobic than rare gases, and the two different kinds of HY are termed intrinsic (rare gases) and extrinsic (alkanes). The HY values of rare gases are proportional to solvent-accessible surface area (ASA), whereas the HY values of alkanes depend on special hydration shells. Earlier work showed that hydration shells produce the hydration energetics of alkanes. Evidence is given here that the transfer energetics of alkanes to cyclohexane [Wolfenden R, Lewis CA, Jr, Yuan Y, Carter CW, Jr (2015) Proc Natl Acad Sci USA 112(24):7484-7488] measure the release of these shells. Alkane shells are stabilized importantly by van der Waals interactions between alkane carbon and water oxygen atoms. Thus, rare gases cannot form this type of shell. The very short (approximately picoseconds) lifetime of the van der Waals interaction probably explains why NMR efforts to detect alkane hydration shells have failed. The close similarity between the sizes of the opposing energetics for forming or releasing alkane shells confirms the presence of these shells on alkanes and supports Kauzmann's 1959 mechanism of protein folding. A space-filling model is given for the hydration shells on linear alkanes. The model reproduces the n values of Jorgensen et al. [Jorgensen WL, Gao J, Ravimohan C (1985) J Phys Chem 89:3470-3473] for the number of waters in alkane hydration shells.
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