Additional file 14: of Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

Figure S13. CW-EPR spectra of the FL and C-terminal deleted (NT-TPR) SGTA proteins. Room Temperature CW-EPR spectra for SGTA FL mutants (blue lines) and corresponding NT-TPR constructs (red lines). CW-EPR spectra mainly provide information about the mobility of the spin labels and thus about the local environment of the labeled residues. Spectra of the FL protein are slightly broader than those corresponding to the C-terminal deletion (NT-TPR), as highlighted by arrows in the figure, suggesting that the absence C-terminal domain increase the overall mobility of the TPR domain. (PDF 559 kb)