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. Author manuscript; available in PMC: 2015 Feb 27.
Published in final edited form as: Cell. 2014 Feb 27;156(5):963–974. doi: 10.1016/j.cell.2014.01.037

Fig. 2. Tau causes specific shift in Hsp90 NMR spectra.

Fig. 2

A, ATP binding modulates the dynamics of the Hsp90-Tau complex. Rainbow representation of 1H-13C-Ile-methyl-TROSY cross-peaks of full-length Hsp90 in complex with Tau (left) and Tau+ATPγS (right). The inset magnifies peaks that sharpen upon ATPγS binding, numbers indicate assigned isoleucines (numbering without N-terminal methionine). B, Tau binding causes shifts and peak doubling in Hsp90 spectra (Hsp90, 125 µM; Tau, 287 µM; Hsp90, black; Hsp90+Tau, red), in the absence and presence of ATPγS (2 mM). The extent of each shift is indicated by a line. See also Fig. S1 and Table S1.