Designability of lattice model heteropolymers.
Protein folds are highly designable, in the sense that many sequences fold to the same conformation. In the present work we derive an expression for the designability in a 20-letter lattice model of proteins which, relying only on the central limit theorem, has a generality which goes beyond the simple model used in its derivation. This expression displays an exponential dependence on the energy of the optimal sequence folding on the given conformation measured with respect to the lowest energy of the conformational dissimilar structures, an energy difference which constitutes the only parameter controlling designability. Accordingly, the designability of a native conformation is intimately connected to the stability of the sequences folding to them.
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Dipartimento di Fisica, Universitá di Milano e INFN Sezione di Milano, via Celoria 16, 20133 Milan, Italy.
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D000465:Algorithms; D001703:Biophysics / Q000379:methods*; D015233:Models, Statistical; D008962:Models, Theoretical; D009154:Mutation; D016011:Normal Distribution; D011108:Polymers; D011487:Protein Conformation
D011108:Polymers