Thermal induced unfolding refolding of a nucleocapsid COVN protein

TL;DR

This study investigates the thermal unfolding and refolding behavior of a nucleocapsid COVN protein, revealing its structural transitions and persistent folds at high temperatures through coarse-grained modeling.

Contribution

It provides new insights into the thermal response and structural stability of the COVN protein using coarse-grained simulations.

Findings

Radius of gyration shows nonmonotonic behavior with temperature.

Protein maintains some folded segments even at high temperatures.

Structural dimensions vary between 1.6 and 2.4 during unfolding.

Abstract

Unfolding of a coarse grained COVN protein from its native configuration shows a linear response with increasing temperature followed by a nonmonotonic double peaks in its radius of gyration. The protein conforms to a random coil of folded segments in native state with increasing tenuous and globular structures in specific temperature regimes where the effective dimensions of corresponding structures D is about 1.6 to 2.4. Thermal agitation alone is not sufficient to fully eradicate its segmental folding as few folds are found to persist around such residues as 65W, 110Y, 224L, 374P even at high temperatures.