Pseudodihedral Potential of Protein Residues and the Prediction of Folding

摘要

The pseudodihedral confromational potential for amino acid residues is evaluated from a statistical analysis of a data set of 300 non homologous crystallized proteins and used in conjunction with a distance-based potential to predict folding from the covalent structure. The results indicate that the inclusion of the conformational propensity per residue in the knowledge-based energy function largely improves the prediction of the native protein folding.