Phys. Rev. Lett. 82, 3372-3375, (1999).
Protein Structures and Optimal Folding from a Geometrical Variational Principle
Cristian Micheletti, Jayanth R. Banavar, Amos Maritan and Flavio Seno
Link to online article.
A novel approach, validated by an analysis of barnase and chymotrypsin
inhibitor, is introduced to elucidate the paramount role played by the
geometry of the protein backbone in steering the folding to the native
state. It is found that native states of proteins, compared with
compact artificial backbones, have an exceedingly large number of
conformations with a given amount of structural overlap with them;
moreover, the density of overlapping conformations, at a given
overlap, of unrelated proteins of the same length are nearly
equal. These results suggest an extremality principle underlying
protein evolution, which, in turn, is shown to be possibly associated
with the emergence of secondary structures.