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A finely tuned interplay between calcium binding, ionic strength and pH modulates conformational and oligomerization equilibria in the Respiratory Syncytial Virus Matrix (M) protein.
Esperante SA, Alvarez-Paggi D, Salgueiro M, Desimone MF, de Oliveira GAP, Arán M, García-Pardo J, Aptekmann AA, Ventura S, Alonso LG, de Prat-Gay G. Esperante SA, et al. Arch Biochem Biophys. 2022 Nov 30;731:109424. doi: 10.1016/j.abb.2022.109424. Epub 2022 Oct 8. Arch Biochem Biophys. 2022. PMID: 36220378
RSV-M undergoes a substantial conformational change at pHs 4.0 to 5.0 that results in the exposure of hydrophobic surfaces, an increase beta sheet content but burial of tryptophan residues. While low ionic strength promotes dimer dissociation at pH 4.0, physiological conce …
RSV-M undergoes a substantial conformational change at pHs 4.0 to 5.0 that results in the exposure of hydrophobic surfaces, an increase beta …