Fig. 3: Interaction between TrxHttex1-39Q and SERF1a by NMR. | Communications Biology

Fig. 3: Interaction between TrxHttex1-39Q and SERF1a by NMR.

From: Amyloid modifier SERF1a interacts with polyQ-expanded huntingtin-exon 1 via helical interactions and exacerbates polyQ-induced toxicity

Fig. 3

a Overlay of HSQC spectra of 15N-labeled SERF1a with increasing ratios of TrxHttex1-39Q. b Residues with larger changes in chemical shift. Peaks in blue were SERF1a alone, and SERF1a with TrxHttex1-39Q at a ratio of 1:2 were labeled in red. c Chemical shift perturbation (CSP) and (d) intensity drop between control and SERF1a with TrxHttex1-39Q (1:2). The signals of residues L9/E42, T18/T59, and E20/R26 were overlapped and unable to be differentiated. Undetected residues were marked in orange. Residues with CSP > 0.1 ppm or residues with normalized intensity drop > 70% were highlighted in blue. e Secondary structure of SERF1a determined by chemical shift index (CSI 3.0). Residues with CSP > 0.1 ppm or residues with normalized intensity drop > 70% were marked with black dots.

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