Figure 4 | Scientific Reports

Figure 4

From: Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation

Figure 4

Intermolecular PRE relaxation experiments for WT lysozyme (40 and 50 °C, 500 MHz) at pH 1.2. Spin-labeled human lysozyme and 15N-isotopically labeled protein were mixed to give a 1:1 molar ratio and R2 relaxation experiments were performed for both paramagnetic and diamagnetic samples. Eight relaxation delay times (8, 13, 18, 23, 28, 38, 48 and 68 ms) were used to collect 1HN-R2 data. (a–c) HSQC spectrum of WT (a), 1HN-R2 (b) and 1HN-Γ2 (c) of the native state peaks at 40 °C. (d–f) HSQC spectrum of WT (d), 1HN-R2 (e) and 1HN-Γ2 (f) of the unfolded state peaks at 50 °C. (g) Structure of WT colored by 1HN-R2 values measured from the unfolded state peaks in (e). Red and green data points in (b,e) indicate 1HN-R2 of the paramagnetic and diamagnetic samples. Red coloring on the lysozyme structure in (g) indicates the regions of the protein that are flexible and predominantly unfolded as indicated by low 1HN-R2 values.

Back to article page