Fig. 4: Ribosome contacts modulate the structure of nascent DHFR without inducing unfolding.
From: Resolving chaperone-assisted protein folding on the ribosome at the peptide level
a, Relative deuterium uptake of FL + 38RNC compared to FL DHFR. DHFR peptides that are protected in the RNC relative to FL DHFR, at any deuteration time point, are colored blue; deprotected peptides are colored red. The Met20 loop is indicated with a green dashed ellipse. See also Extended Data Fig. 6a and Supplementary Data 1. b, Oxidoreductase activity of 25 nM FL DHFR, empty 70S ribosomes without an NC or RNCs. Where indicated, reactions are supplemented with 50 µg ml−1 RNaseA and 50 mM EDTA, a peptide corresponding to the C terminus of DHFR (C10, SYCFEILERR) or a scrambled-sequence control peptide (Scr, RFIERCELYS). Data are presented as mean values; error bars, s.d.; n = 3 independent experiments.
