Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 122, Issue 13, Pages 3635-3646Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.7b12060
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Funding
- National Science Foundation [UPENN MRSEC DMR 11-20901, CBET 1652646, CHE 1665339]
- Alfred P. Sloan Research Foundation
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The solubility of proteins and other macromolecular solutes plays an important role in numerous biological, chemical, and medicinal processes. An important determinant of protein solubility is the solvation free energy of the protein, which quantifies the overall strength of the interactions between the protein and the aqueous solution that surrounds it. Here we present an all-atom explicit-solvent computational framework for the rapid estimation of protein solvation free energies. Using this framework, we estimate the hydration free energy of hydrophobin II, an amphiphilic fungal protein, in a computationally efficient manner. We further explore how the protein hydration free energy is influenced by enhancing flexibility and by the addition of sodium chloride, and find that it increases in both cases, making protein hydration less favorable.
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