A method for prediction of the secondary structure of a protein from its primary structure. A survey of proteins of known secondary and tertiary structure allows an empirical classification of amino acid residues according to their abilities to strengthen or destabilise α-helix or β-structure. Recent advances have high-speed computers using Monte Carlo calculations to first fit multi-helix proteins into individual α-helices, then use empirically assigned interaction coefficients to locate the helices in spatial relation to each other.