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Multibody correlations in the hydrophobic solvation of glycine peptides
Protein collapse during folding is often assumed to be driven by a hydrophobic solvation energy (ΔG(vdw)) that scales linearly with solvent-accessible surface area (A). In a previous study, we argued that ΔG(vdw), as well as its attractive (ΔG(att)) and repulsive (ΔG(rep)) components, was not simply...
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| Veröffentlicht in: | J Chem Phys |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
American Institute of Physics
2014
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4257976/ https://ncbi.nlm.nih.gov/pubmed/25494796 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1063/1.4901886 |
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