Crystal nucleation for a model of globular proteins

Area of Science:

• Physical Chemistry
• Biophysics
• Computational Chemistry

Background:

• The Talanquer and Oxtoby continuum model provides a framework for studying globular protein behavior.
• Understanding protein phase transitions is crucial for various biological and chemical processes.
• Metastable fluid-fluid coexistence and nucleation phenomena are key areas in soft matter physics.

Purpose of the Study:

• To numerically investigate the Talanquer and Oxtoby continuum model for globular proteins.
• To analyze the model's validity near the metastable fluid-fluid coexistence curve.
• To develop an approximate analytic solution for nucleating crystal droplets.

Main Methods:

• Numerical simulations of the continuum model.
• Analysis of the metastable fluid-fluid coexistence region.
• Derivation of an approximate analytic solution for crystal droplet properties.

Main Results:

• Classical nucleation theory is demonstrated to be invalid near the metastable critical point.
• Classical nucleation theory also fails close to the liquidus line.
• An approximate analytic solution for the shape and properties of nucleating crystal droplets was obtained.

Conclusions:

• The limitations of classical nucleation theory in protein systems are highlighted.
• The study provides insights into the behavior of globular proteins in metastable states.
• The developed analytic solution offers a tool for further theoretical and experimental investigations.