Author: Nila Roy Choudhury; Gregory Heikel; Maryia Trubitsyna; Peter Kubik; Jakub Stanislaw Nowak; Shaun Webb; Sander Granneman; Christos Spanos; Juri Rappsilber; Alfredo Castello; Gracjan Michlewski
Title: RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination Document date: 2017_10_9
ID: ifla4aix_11
Snippet: Tm (43 C o ) in a thermal denaturation assay ( Figure S1b ). Furthermore, using Size Exclusion Chromatography with Multi-Angle Light Scattering (SEC-MALS), we established that there was no difference in the elution profiles between the wild-type and the mutant protein ( Figure S1c ). The MALS-measured mass distribution for His-TRIM25 was 263 ± 5.3 kDa, with an Mw/Mn of ~ 1.01. The His-TRIM25ΔRBD had values of 258 ± 5 kDa, and ≥ 1.003 Mw/Mn.....
Document: Tm (43 C o ) in a thermal denaturation assay ( Figure S1b ). Furthermore, using Size Exclusion Chromatography with Multi-Angle Light Scattering (SEC-MALS), we established that there was no difference in the elution profiles between the wild-type and the mutant protein ( Figure S1c ). The MALS-measured mass distribution for His-TRIM25 was 263 ± 5.3 kDa, with an Mw/Mn of ~ 1.01. The His-TRIM25ΔRBD had values of 258 ± 5 kDa, and ≥ 1.003 Mw/Mn. This suggests that both wild type and TRIM25ΔRBD formed tetramers in our preparation.
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