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Fig. 6 | BMC Biology

Fig. 6

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

Fig. 6

SGTA C-terminal domain is able to dimerise in the full-length context II. a Calculated correlations times (τc) for N-terminal (blue) and TPR (maroon) domains in the context of different SGTA constructs (n values and further data in Additional file 12: Figure S11). b Detail of 1H-15N HSQC spectra for different SGTA constructs showing two amide signals from the N-terminal domain (blue) and two signals from the TPR domain (maroon). Note severe broadening effect of TPR signals in FLΔQ and FL constructs. c DEER measurements and distances determined for FL and NT-TPR SGTA constructs spin labeled in S88C and S197C mutants. (i) Primary frequency-domain DEER data. (ii) Background-corrected dipolar evolution data (black lines) and corresponding fits obtained through DeerAnalysis2016 [49] by Tikhonov regularization. (iii) Distance distributions obtained by Tikhonov regularization. Blue fits: FL SGTA; red fits: NT-TPR construct

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