STABILITY THRESHOLD AS A SELECTION PRINCIPLE FOR PROTEIN DESIGN

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.

• Publication year

  1997

• Venue

  Physical Review Letters

• Publication date

  1997-04-20

• Fields of study

  Biology, Physics

• Identifiers
  DOI 10.1103/PhysRevLett.78.3967arXiv cond-mat/9704167
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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