Stability of Designed Proteins Against Mutations

Abstract

The stability of model proteins with designed sequences is assessed in terms of the number of sequences (obtained from the designed sequence through mutations), which fold into 5the ``native'' conformation. By a complete enumeration of the total number of sequences obtained by introducing up to 4 point mutations and up to 7 composition--conserving mutations (swapping of amino acids) in a 36mers chain, it is found that there are $10^8-10^9$ sequences which in the folding process target onto the ``native'' conformation. Consequently, proteins with designed sequences display a remarkable degree of stability and, to a large extent, of designability.

References in corpus (4)

• Chain length scaling of protein folding time
• Reply to Comment on "Criterion that Determines the Foldability of Proteins"
• Folding and Misfolding of Designed Heteropolymer Chains with Mutations
• How Accurate Must Potentials Be for Successful Modeling of Protein Folding?

Cited by in corpus (9)

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• Thermodynamics of Neutral Protein Evolution
• Stability and the Evolvability of Function in a Model Protein
• On Hydrophobicity Correlations in Protein Chains
• Designability of lattice model heteropolymers
• Dynamical chaos and power spectra in toy models of heteropolymers and proteins
• Synthesizing a Clock Signal with Reactions---Part I: Duty Cycle Implementation Based on Gears
• Selecting fast folding proteins by their rate of convergence
• Native state of natural proteins optimises local entropy