Highly Designable Protein Structures and Inter Monomer Interactions

TL;DR

This study uses computational methods to analyze protein designability and inter-monomer interactions, revealing how interaction strength influences structure stability and mutation sensitivity in a simplified lattice model.

Contribution

It introduces a detailed analysis of how interaction potential parameters affect protein structure designability and mutation effects in a lattice model.

Findings

Designability depends on interaction potential strength.

Unique ground states are mutation-sensitive.

Higher non-additive interaction strength increases designability.

Abstract

By exact computer enumeration and combinatorial methods, we have calculated the designability of proteins in a simple lattice H-P model for the protein folding problem. We show that if the strength of the non-additive part of the interaction potential becomes larger than a critical value, the degree of designability of structures will depend on the parameters of potential. We also show that the existence of a unique ground state is highly sensitive to mutation in certain sites.