The crystallization of asymmetric patchy models for globular proteins in solution

TL;DR

This paper studies how asymmetry in patch geometry and bond energy affects the phase behavior and nucleation of asymmetric patchy models for globular protein crystallization, providing insights into optimizing crystallization conditions.

Contribution

It reveals that energy asymmetry significantly impacts crystallization, while geometry asymmetry has a weaker effect, informing strategies for protein crystallization.

Findings

Energy asymmetry markedly affects thermodynamics and kinetics.

Geometry asymmetry has a weak influence.

Results support and refine existing crystallization theories.

Abstract

Asymmetric patchy particle models have recently been shown to describe the crystallization of small globular proteins with near quantitative accuracy. Here, we investigate how asymmetry in patch geometry and bond energy generally impact the phase diagram and nucleation dynamics of this family of soft matter models. We find the role of the geometry asymmetry to be weak, but the energy asymmetry to markedly interfere with the crystallization thermodynamics and kinetics. These results provide a rationale for the success and occasional failure of George and Wilson's proposal for protein crystallization conditions as well as physical guidance for developing more effective protein crystallization strategies.