Skip to main content
Fig. 3 | BMC Biology

Fig. 3

From: Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

Fig. 3

Biophysical characterization of SGTA C-terminal domain. a Far UV CD spectra of the C-terminal domain of SGTA (top), its version lacking the glutamine-rich region (middle) and the C-terminal mutated in the NNP region (bottom). b 1H-15N TROSY HSQC of the deuterated version of SGTA C-terminal domain with partial assignment. c, d Native mass spectrometry spectra of the C-terminal domain of SGTA (c) and of the SGTA 3xNNP/AAA C-terminal mutant (d). Peaks corresponding to the same species are marked with colored circles with the charge number written inside. The theoretical molecular weight appears under the title and the obtained molecular weights for each species are shown on the right in the same color scheme

Back to article page