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>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 <italic>D &ap; 1.6&ndash;2.4</italic>. 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.