Hydrophobicity of proteins and nanostructured solutes is governed by topographical and chemical context

Hydrophobic interactions drive many important biomolecular self-assembly phenomena. However, characterizing hydrophobicity at the nanoscale has remained a challenge due to its nontrivial dependence on the chemistry and topography of biomolecular surfaces. Here we use molecular simulations coupled wi...

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Bibliographic Details
Published in:Proc Natl Acad Sci U S A
Main Authors: Xi, Erte, Venkateshwaran, Vasudevan, Li, Lijuan, Rego, Nicholas, Patel, Amish J., Garde, Shekhar
Format: Artigo
Language:Inglês
Published: National Academy of Sciences 2017
Subjects:
Chemical Physics of Water Special Feature
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC5754750/
https://ncbi.nlm.nih.gov/pubmed/29158409
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1700092114
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