Figure 3: Structural destabilization of nitrosylated UCHL1. | Scientific Reports

Figure 3: Structural destabilization of nitrosylated UCHL1.

From: S-nitrosylation of UCHL1 induces its structural instability and promotes α-synuclein aggregation

Figure 3

Circular dichroism spectroscopy, bars showing secondary structural content of (a) UCHL1 and nitrosylated UCHL1 (b) TM and nitrosylated TM (c,d,e) 2D [15N,1H] HSQC spectrum of UCHL1 (0.2 mM protein, 100 mM Tris-HCl, pH 7.4, 298 K) exhibiting expected number of resonances with excellent chemical shift dispersion, indicative of a well-folded protein. (c) Overlay of 2D [15N,1H] HSQC spectra of UCHL1 (blue) and TM (red). Substantial line broadening of resonances was observed and poor dispersion of amide proton resonances in a narrow spectral region around 7.5–9 ppm is indicative of partially unfolded/aggregated protein. (d) Overlay of 2D [15N,1H] HSQC spectra of nitrosylated UCHL1 (blue) and UCHL1 (red) (e) Overlay of 2D [15N,1H] HSQC spectra of nitrosylated TM (blue) overlapped with TM as control (red).

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