Thermal induced unfolding refolding of a nucleocapsid COVN protein

2020/04/01 by Warin Rangubpit, Rangubpit, Warin, Pornthep Sompornpisut +3
Biochemistry, Genetics and Molecular Biology · Materials Science · #Biological Physics (physics.bio-ph) #Biomolecules (q-bio.BM) #Enzyme Structure and Function #FOS: Biological sciences #FOS: Physical sciences #Hemoglobin structure and function #Protein Structure and Dynamics #Soft Condensed Matter (cond-mat.soft)

paper · pdf · doi:10.48550/arxiv.2004.00581

openalex publication_date 2020/04/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28

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.

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