Fig. 2: Condensates formed by different chimeric proteins modulate NOX enzymatic activity.
From: Local environment in biomolecular condensates modulates enzymatic activity across length scales
A Representative profile of the reaction progress characterized by a decrease in the NADH absorbance at 340 nm for the homogeneous solution (black symbols, NOX) and the heterogeneous system composed of condensates and the dilute phase (blue symbols, Dbp1-NOX, red symbols, Laf1-NOX and green symbols, Ddx4-NOX). Proteins were diluted to 1 µM in 25 mM Tris, 20 mM NaCl pH 7.5. B Initial rates measured for the NOX homogeneous system (gray bar) and for the heterogeneous systems (“Total (2 phases)”) at 1 µM in 25 mM Tris, 20 mM NaCl pH 7.5. n ≥ 3 independent experiments. Data were presented as mean values ± SEM. C Initial rates of 1 µM protein solutions at high ionic strength (500 mM NaCl), where a single homogeneous phase was observed for all proteins. n ≥ 3 independent experiments. Data were presented as mean values ± SEM. D Mass distribution of 20 nM NOX and Dbp1-NOX solutions at low ionic strength (20 mM NaCl) analyzed by single-molecule mass photometry. Both peaks correspond to the dimeric forms of the protein: 45 kDa for NOX and 79 kDa for Dbp1-NOX. E Initial rates of the homogeneous systems at 20 nM enzyme (c«csat) and low ionic strength (20 mM NaCl). n = 3 independent experiments. Data were presented as mean values ± SEM. Created with BioRender.com.
