The Origin of the Designability of Protein Structures

TL;DR

This study investigates factors influencing the designability of lattice protein structures, finding that chain length and hydrophobic core formation are key, while lattice bipartiteness is not a main factor.

Contribution

It provides new insights into the determinants of protein structure designability, emphasizing the importance of chain length and hydrophobic core development.

Findings

Bipartiteness of the lattice is not a main factor in designability.

Longer chains tend to have more highly designable structures.

Hydrophobic core formation is crucial for designability.

Abstract

We examined what determines the designability of 2-letter codes (H and P) lattice proteins from three points of view. First, whether the native structure is searched within all possible structures or within maximally compact structures. Second, whether the structure of the used lattice is bipartite or not. Third, the effect of the length of the chain, namely, the number of monomers on the chain. We found that the bipartiteness of the lattice structure is not a main factor which determines the designability. Our results suggest that highly designable structures will be found when the length of the chain is sufficiently long to make the hydrophobic core consisting of enough number of monomers.