Globular bundles and entangled network of proteins (CorA) by a coarse-grained Monte Carlo simulation

TL;DR

This study uses a coarse-grained Monte Carlo simulation to explore how protein assemblies, like CorA, form globular bundles or entangled networks across different concentrations and temperatures, revealing distinct structural behaviors.

Contribution

It introduces a novel coarse-grained simulation approach to analyze multi-scale protein assembly morphologies and their dependence on concentration and temperature.

Findings

Native phase shows stable radius of gyration for proteins.

Denatured phase exhibits significant growth in protein radius of gyration with concentration.

Inner segments maintain consistent size, indicating their role in self-organization.

Abstract

Using a coarse-grained model, self-organized assembly of proteins (e.g. CorA and its inner segment iCorA) is studied by examining quantities such as contact profile, radius of gyration, and structure factor as a function of protein concentration at a range of low (native phase) to high (denature phase) temperatures. Visual inspections show distinct structures, i.e. isolated globular bundles to entangled network on multiple length scales in dilute to crowded protein concentrations. In native phase, the radius of gyration of the protein does not vary much with the protein concentration while that of its inner segment increases systematically. In contrast, the radius of gyration of the protein shows enormous growth with the concentration due to entanglement while that of the inner segment remains almost constant in denatured phase. The multi-scale morphology of the collective assembly is quantified by estimating the effective dimension D of protein from scaling of the structure factor: collective assembly from inner segments remains globular (D aroud 3) at almost all length scales in its native phase while that from protein chains shows sparsely distributed morphology with D around 2 in entire temperature range due to entanglement except in crowded environment at low temperature where D around 2.6. Higher morphological response of chains with only the inner-segments due to selective interactions in its native phase may be more conducive to self-organizing mechanism than that of the remaining segments of the protein chains.