We present a meanfield theoretical approach for studying protein-solvent interactions. Starting with the partition function of the system, we develop a field theory by introducing densities for the different components of the system. At this point, protein-solvent interactions are introduced following the inhomogeneous Flory-Huggins model for polymers. Finally, we calculate the free energy in a meanfield approximation. We apply this method to study the stability of the tetramerization domain of the tumor suppressor protein p53 when subjected to site-directed mutagenesis. The four chains of this protein are held together by hydrophobic interactions, and some mutations can weaken this bond while preserving the secondary structure of the single protein chains. We find good qualitative agreement between our numerical results and experimental data, thus encouraging the use of this method as a guide in designing experiments.
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| http://dx.doi.org/10.1016/S0006-3495(01)76125-5 | DOI Listing |
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