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. 2009 Feb 17;7(2):e1000034. doi: 10.1371/journal.pbio.1000034

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© 2009 Mukrasch et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Superposition of a selected portion of the ¹H-¹⁵N HSQC spectra of htau40 in the free state (blue) and in the presence of MTs (red). Resolved peaks are labelled with their assignments. The tau:tubulin heterodimer ratio was 2:1. To highlight changes in NMR signal intensities, a trace through the center (solid line) of selected peaks is shown.

(B) NMR signal intensity ratios between signals observed for htau40 in the MT-bound and in the free state. Repeat boundaries are indicated by vertical dashed lines. Hot spots of binding are highlighted in blue.

(C) Absolute magnitude of ¹⁵N chemical shift changes. The estimated error based on ¹H-¹⁵N HSQCs of two different htau40 samples was 0.025 ppm.

(D,E) NMR signals intensity ratios in the proline-rich regions (D) and in the repeat domain (E). Values were taken from (B). In (E), the position of the two hexapeptides is indicated by black bars.