Structural Determinant of Protein Designability

Preprint
Publisher Website
Google Scholar
  • 23 August 2002
Abstract
Here we present an analytical theory for the relationship between a protein structure's contact matrix and the shape of its energy spectrum in amino acid sequence space. We demonstrate a dependence of the number of sequences of low energy in a structure on the eigenvalues of the structure's contact matrix, and then confirm the validity of our analytical result using a Monte Carlo simulation. We find that the structures with the most low-energy sequences exhibit some striking symmetries and regularities reminiscent of protein secondary structure. We argue that given sufficiently strict requirements for foldability, these structures are the most designable.

This publication has 0 references indexed in Scilit: