Structural studies of Cardiovirus 2A protein reveal the molecular basis for RNA recognition and translational control

Published: 7 December 2020| Version 1 | DOI: 10.17632/gkpwngy65h.1
Contributor:
Neva Caliskan

Description

Raw data related to Figure 2 and 5 Capillary scans and thermophoretic time-traces of microscale thermophoresis (MST) measurements of binding between EMCV 2A and A) EMCV RNA 1, B) EMCV RNA 2, C) EMCV RNA 3, D) EMCV RNA 4, E) EMCV RNA 5, F) EMCV RNA 5, G) EMCV RNA 6, H) 30S, I) 50S, J) 40S, K) 60S, L) 70S and M) 70S IC. The protein was fluorescently labelled, while unlabeled ligands were added at different concentrations. The grey boxes in the capillary scans mark 20% above and below the average peak fluorescence, the acceptable limit of deviations across the fluorescence scans. Blue and red boxes in the time-course traces represent the temperature jump and MST-on time (10s), respectively. In all cases, there is no adsorption of the labeled protein to the capillaries. See Fig. 2 and Fig. 5 for the resulting binding curves.

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Institutions

  • Helmholtz-Zentrum fur Infektionsforschung GmbH
  • Helmholtz-Institut fur RNA-basierte Infektionsforschung

Categories

Thermophoresis, Optical Tweezer

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