Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 43, Pages 17678-17683Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1110703108
Keywords
binding; hydrophobicity; thermodynamics
Categories
Funding
- National Institutes of Health [R01-GM078102-04]
- National Science Foundation [CBET-0933169, CBET-1134341, NSF-CBET-0967937]
- Office of Science, Office of Basic Energy Sciences, Materials Sciences and Engineering Division and Chemical Sciences, Geosciences, and Biosciences Division of the US Department of Energy [DE-AC02-05CH11231]
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [1134341] Funding Source: National Science Foundation
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Interfaces are a most common motif in complex systems. To understand how the presence of interfaces affects hydrophobic phenomena, we use molecular simulations and theory to study hydration of solutes at interfaces. The solutes range in size from subnanometer to a few nanometers. The interfaces are self-assembled monolayers with a range of chemistries, from hydrophilic to hydrophobic. We show that the driving force for assembly in the vicinity of a hydrophobic surface is weaker than that in bulk water and decreases with increasing temperature, in contrast to that in the bulk. We explain these distinct features in terms of an interplay between interfacial fluctuations and excluded volume effects-the physics encoded in Lum-Chandler-Weeks theory [Lum K, Chandler D, Weeks JD (1999) J Phys Chem B 103:4570-4577]. Our results suggest a catalytic role for hydrophobic interfaces in the unfolding of proteins, for example, in the interior of chaperonins and in amyloid formation.
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