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. Author manuscript; available in PMC: 2011 Feb 1.
Published in final edited form as: Nat Struct Mol Biol. 2010 Jul 11;17(8):939–947. doi: 10.1038/nsmb.1873

Figure 4.

Figure 4

NMR Solution studies of Lys11-linked diubiquitin.

(a) Overlay of 15N,1H HSQC spectra of ubiquitin K63R (red) onto Lys11-linked diubiquitin K63R (blue). The expansion illustrates the doubling of peaks observed for Lys29, Ile30, Asp32 and Lys33. The signal for Asp52 is unperturbed. (b, c) Weighted chemical shift perturbation according to residue number for Lys11-linked diubiquitin with both molecules 13C, 15N–labeled (blue, K63R ubiquitin mutant) or only labeled distally (orange, K11R ubiquitin mutant). Shown are chemical shift perturbations observed for doubled peaks calculated as the weighted difference between the chemical shift position in the Lys11-linked diubiquitin mutants and their respective monoubiquitin counterparts at pH7.2 (b) and pH 3.5 (c). Stars (*) indicate exchange broadened residues, and arrows indicate K29 and K33. (d) Combined chemical shift perturbation differences for Lys48- and Lys63-linked diubiquitin. This data was kindly provided by Takeshi Tenno 22.