Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding

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dc.contributor.authorHuang, D.M.
dc.contributor.authorChandler, D.
dc.date.issued2000
dc.description.abstractThe Lum–Chandler–Weeks theory of hydrophobicity [Lum, K., Chandler, D. & Weeks, J. D. (1999) J. Phys. Chem. 103, 4570–4577] is applied to treat the temperature dependence of hydrophobic solvation in water. The application illustrates how the temperature dependence for hydrophobic surfaces extending less than 1 nm differs significantly from that for surfaces extending more than 1 nm. The latter is the result of water depletion, a collective effect, that appears at length scales of 1 nm and larger. Because of the contrasting behaviors at small and large length scales, hydrophobicity by itself can explain the variable behavior of entropies of protein folding.
dc.description.statementofresponsibilityDavid M. Huang and David Chandler
dc.identifier.citationProceedings of the National Academy of Sciences of USA, 2000; 97(15):8324-8327
dc.identifier.doi10.1073/pnas.120176397
dc.identifier.issn0027-8424
dc.identifier.issn1091-6490
dc.identifier.orcidHuang, D.M. [0000-0003-2048-4500]
dc.identifier.urihttp://hdl.handle.net/2440/129941
dc.language.isoen
dc.publisherNational Academy of Sciences
dc.relation.replaceshttp://hdl.handle.net/2440/87359
dc.relation.replaces2440/87359
dc.rightsCopyright © The National Academy of Sciences
dc.source.urihttps://doi.org/10.1073/pnas.120176397
dc.subjectSolutions
dc.subjectTemperature
dc.subjectEnergy Transfer
dc.subjectProtein Folding
dc.titleTemperature and length scale dependence of hydrophobic effects and their possible implications for protein folding
dc.typeJournal article
pubs.publication-statusPublished

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