Figure 5 | Scientific Reports

Figure 5

From: The N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State

Figure 5

CEST experiments probing the binding equilibrium of NTAc-αS. CEST 1H-15N HSQC spectra were recorded by applying a continuous wave saturation (170 Hz or 350 Hz) on the 15N resonance with offsets ranging from −28 kHz to + 28 kHz, and using a reference spectrum measured with an offset of 100 kHz. Measurements were carried out using a protein concentration of 300 μM and 0.06% (0.6 mg/ml) of SUVs composed of DOPE:DOPS:DOPC lipids in a ratio of 5:3:2 (w/w). (a,b) CEST surfaces measured using bandwidths of 350 Hz and 170 Hz, respectively. (c,d) CEST saturation along the αS sequence measured using bandwidths of 350 Hz and 170 Hz, respectively. Black, red and green lines refer to the averaged CEST profiles measured using offsets at + /− 1.5 kHz, + /− 3 kHz and + /− 5 kHz, respectively.

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