Stability Threshold as a Selection Principle for Protein Design
arXiv:cond-mat/9704167 · doi:10.1103/PhysRevLett.78.3967
Abstract
The sensitivity of the native states of protein-like heteropolymers to mutations modelled as perturbations in the interaction potential between amino acids is studied. The stability threshold against mutations is shown to be zero for random heteropolymers on a lattice in two dimensions, whereas a design procedure modelling evolution produces a non-zero threshold. We introduce an evolution-like protein design procedure based on an optimization of the stability threshold that is shown to naturally ensure thermodynamic stability as well.
4 pages, RevTex, 4 figures included, to appear on Phys. Rev. Lett
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