How optimization of potential functions affects protein folding.

AUTOR(ES)

Hao, M H

RESUMO

The relationship between the optimization of the potential function and the foldability of theoretical protein models is studied based on investigations of a 27-mer cubic-lattice protein model and a more realistic lattice model for the protein crambin. In both the simple and the more complicated systems, optimization of the energy parameters achieves significant improvements in the statistical-mechanical characteristics of the systems and leads to foldable protein models in simulation experiments. The foldability of the protein models is characterized by their statistical-mechanical properties--e.g., by the density of states and by Monte Carlo folding simulations of the models. With optimized energy parameters, a high level of consistency exists among different interactions in the native structures of the protein models, as revealed by a correlation function between the optimized energy parameters and the native structure of the model proteins. The results of this work are relevant to the design of a general potential function for folding proteins by theoretical simulations.

Documentos Relacionados

• Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding.
• Submillisecond events in protein folding.
• A speed limit for protein folding.
• Temperature dependence of the hydrophobic interaction in protein folding.
• Spin glasses and the statistical mechanics of protein folding.