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, 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.Comment: in press on Phys. Rev.

The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor

An analogue of the BPTI folding intermediate that contains only the disulphide bond between Cys-5 and Cys-55 has been prepared by mutation or the other four Cys residues to Ser. On the basis of its circular dichroism and 1H-nuclear magnetic resonance spectra and its electrophoretic mobility, this intermediate is shown to be at least partially folded at low temperatures. This probably accounts for several of the unique properties of this intermediate observed during folding

The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor

An analogue of the BPTI folding intermediate that contains only the disulphide bond between Cys-5 and Cys-55 has been prepared by mutation or the other four Cys residues to Ser. On the basis of its circular dichroism and 1H-nuclear magnetic resonance spectra and its electrophoretic mobility, this intermediate is shown to be at least partially folded at low temperatures. This probably accounts for several of the unique properties of this intermediate observed during folding.</p