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A large number of proteins, found experimentally to havedifferent optimum pH of maximal stability, were studied toreveal the basic principles of their preferenence for a par-ticular pH. The pH-dependent free energy of folding wasmodeled numerically as a function of pH as well as the netcharge of the protein. The optimum pH was determined inthe numerical calculations as the pH of the minimum freeenergy of folding. The experimental data for the pH ofmaximal stability (experimental optimum pH) was repro-ducible (rmsd¼0.73)....
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Báo cáo khóa học: Numerical calculations of the pH of maximal protein stability
