The computational techniques of sorting out protein folds (these techniques include dynamic programming, self-consistent field theory, etc.) have already ceased to be the bottleneck of predictions. The main problem is that all the methods of recognition and prediction of protein structure can actually use only some part of the interactions operating in the chain, and that even their energies are not known precisely. This is the principal source of errors now. The errors can be reduced by employment of many distant homologues, but this opens a possibility to predict a generalized folding pattern rather than a particular fold with all its details.