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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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| 出版年: | Proc Natl Acad Sci U S A |
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| 主要な著者: | , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
National Academy of Sciences
2017
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| 主題: | |
| オンライン･アクセス: | 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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