Huaying Zhao
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Evolution of a fuzzy ribonucleoprotein complex in viral assembly
eLife Assessment This is a valuable study that combines biophysical and evolutionary approaches to understand why particular mutations in the SARS-CoV-2 protein N arose during the COVID-19 pandemic. The evidence is solid and supports the conclusions.
Evolution of a fuzzy ribonucleoprotein complex in viral assembly
Abstract SARS-CoV-2 assembly entails condensation of viral RNA by the viral nucleocapsid (N) protein into ribonucleoprotein particles (RNPs). Lacking high-resolution structural information, biochemical and biophysical approaches have revealed their architectural principles, which involve cooperative interactions of several protein-protein and protein-RNA interfaces, initiated through oligomerization of conserved transient helices in the central disordered linker of N.
Modulation of biophysical properties of nucleocapsid protein in the mutant spectrum of SARS-CoV-2
Request a detailed protocol CD spectra were acquired in a Chirascan Q100 (Applied Photophysics, UK), using cuvettes of 1 mm pathlength, and data acquisition with 1 nm steps and 1 s integration time. Results are averages of three acquisitions, corrected for buffer background. Protein concentration was 3 µM in buffer LS, except No in buffer HS. For the acquisition of fluorescence spectra, protein samples at 1 µM were loaded into a quartz cuvette with 1.0 cm optical pathlength.
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