Stability Threshold as a Selection Principle for Protein Design

Preprint

20 April 1997

preprint
Published by arXiv in arXiv

https://doi.org/10.48550/arXiv.cond-mat/9704167

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.

Keywords

SELECTION PRINCIPLE
STABILITY THRESHOLD
MODELLING EVOLUTION
HETEROPOLYMERS
PROTEIN DESIGN
NATIVE STATES
THRESHOLD
MUTATIONS

All Related Versions

Version 1, 1997-04-20, ArXiv
Published version: Physical Review Letters, 78 (20), 3967.

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