Thermal-induced unfolding-refolding of a nucleocapsid COVN protein

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