Pair interactions sequence-structure-function prediction

Once a successful set of rules for the folding of all a proteins is available, we can turn our attention to the known mainly a, a/jS and mainly p proteins and find, from a statistical analysis of their structures, which pairs of side chains destabilize helix-helix interactions and result in jS-sheet formation (previous investigations indicate that Phe-Phe, Phe-Tyr, Glu-Arg and Glu-Lys pairs are probable candidates for helix-helix destabilizers ). The rules thus derived from all the known protein structures can then be applied to the prediction of the three dimensional fold and packing of the secondary structures of other amino acid sequences whose structures are not known, that is, to the prediction of a cursory but full three-dimensional structure of a protein, which may be further refined by the application of standard potential energy functions. 

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