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Direct measurement of Stokes–Einstein diffusion of Cowpea mosaic virus with 19 µs-resolved XPCS
Brownian motion of Cowpea mosaic virus (CPMV) in water was measured using small-angle X-ray photon correlation spectroscopy (SA-XPCS) at 19.2 µs time resolution. It was found that the decorrelation time τ(Q) = 1/DQ (2) up to Q = 0.091 nm(−1). The hydrodynamic radius R (H) determined from XPCS using...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9641563/ https://www.ncbi.nlm.nih.gov/pubmed/36345751 http://dx.doi.org/10.1107/S1600577522008402 |
Sumario: | Brownian motion of Cowpea mosaic virus (CPMV) in water was measured using small-angle X-ray photon correlation spectroscopy (SA-XPCS) at 19.2 µs time resolution. It was found that the decorrelation time τ(Q) = 1/DQ (2) up to Q = 0.091 nm(−1). The hydrodynamic radius R (H) determined from XPCS using Stokes–Einstein diffusion D = kT/(6πηR (H)) is 43% larger than the geometric radius R (0) determined from SAXS in the 0.007 M K(3)PO(4) buffer solution, whereas it is 80% larger for CPMV in 0.5 M NaCl and 104% larger in 0.5 M (NH(4))(2)SO(4), a possible effect of aggregation as well as slight variation of the structures of the capsid resulting from the salt–protein interactions. |
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