Computer simulation of protein solvation, hydrophobic mapping, and the oxygen effect in radiation biology

摘要

Hydrophobic effects are central to the structural stability of biomolecules, particularly proteins, in solution but are not understood at a molecular level. This project developed a new theoretical approach to calculation of hydrophobic effects. This information theory approach can be implemented with experimental, including computer simulation-experimental, information. The new theory is consistent with, builds upon, and subsumes previous integral equation and scaled particle statistical thermodynamic modes of hydrophobic effects. The new theory is sufficiently simple to permit application directly to complex biomolecules in solution and to permit further expansion to incorporate more subtle effects.