Mesoscopic model for mechanical characterization of biological protein materials

TL;DR

This paper introduces a mesoscopic model using Go potential to analyze the elastic behavior of biological protein materials, linking native topology to mechanical resilience and providing insights consistent with experimental data.

Contribution

The study develops a novel mesoscopic modeling approach for protein materials that incorporates native topology effects and offers quantitative predictions of mechanical properties.

Findings

Parallel hydrogen bonds enhance mechanical resilience.

The model's predictions align with experimental and atomistic data.

Native topology significantly influences protein mechanical behavior.

Abstract

Mechanical characterization of protein molecules has played a role on gaining insight into the biological functions of proteins, since some proteins perform the mechanical function. Here, we present the mesoscopic model of biological protein materials composed of protein crystals prescribed by Go potential for characterization of elastic behavior of protein materials. Specifically, we consider the representative volume element (RVE) containing the protein crystals represented by alpha-carbon atoms, prescribed by Go potential, with application of constant normal strain to RVE. The stress-strain relationship computed from virial stress theory provides the nonlinear elastic behavior of protein materials and their mechanical properties such as Young's modulus, quantitatively and/or qualitatively comparable to mechanical properties of biological protein materials obtained from experiments and/or atomistic simulations. Further, we discuss the role of native topology on the mechanical properties of protein crystals. It is shown that parallel strands (hydrogen bonds in parallel) enhances the mechanical resilience of protein materials.