Unfolding designable structures

TL;DR

This paper investigates the relationship between the designability of protein folds and their stability, showing that more designable structures are easier to unfold, using lattice models and Langevin dynamics.

Contribution

It applies the 2D hydrophobic-polar lattice model and Langevin dynamics to classify and analyze the unfolding properties of protein-like structures based on their designability.

Findings

More designable folds are easier to unfold.

Designability correlates with the number of surface-core bonds.

Selected folds are intrinsically more stable.

Abstract

Among an infinite number of possible folds, nature has chosen only about 1000 distinct folds to form protein structures. Theoretical studies suggest that selected folds are intrinsically more designable than others; these selected folds are unusually stable, a property called the designability principle. In this paper we use the 2D hydrophobic-polar lattice model to classify structures according to their designability, and Langevin dynamics to account for their time evolution. We demonstrate that, among all possible folds, the more designable ones are easier to unfold due to their large number of surface-core bonds.