NMR chemical shift assignment of mitochondrial yeast Tim9, Tim10 and Tim12 proteins in the reduced (disulfides broken) and oxidized (disulfides formed) forms

Published: 1 March 2020| Version 1 | DOI: 10.17632/b3n93f3bcr.1
Paul Schanda


Solution-state NMR chemical shift assignments of the small Tim chaperone subunits in their unassembled form. The three proteins are: S. cerevisiae Tim9 (UniProtKB - O74700 (TIM9_YEAST)) S. cerevisiae Tim10 (UniProtKB - P87108 (TIM10_YEAST)) S. cerevisiae Tim12 (UniProtKB - P32830 (TIM12_YEAST)) The proteins were in each case "isolated", i.e. for example in samples of Tim9, no Tim10 or Tim12 was present. Two different samples states were investigated for each of the three proteins, with the cysteines in the conserved CX3C motifs either forming disulfides ("oxidized") or not ("reduced"); these states have been obtained by not adding or adding reducing agent TCEP (see below). Sample temperature: 298 K. Sample buffer: 20 mM MES (2-(N- morpholino)ethanesulfonic acid) pH 6.5, 50 mM NaCl. In the samples labeled as "reduced", additionally 10 mM tris(2-carboxyethyl)phosphine (TCEP) was added. Details are provided in Weinhäupl, Lindau, Wang, Melchionda, Hessel, Brennich, Lindorff-Larsen, Wiedemann, Schanda; 2020 (submitted). All deposited files are in TALOS format, and have been used to determine the alpha-helical structure propensity in the manuscript above.



Institut de Biologie Structurale


Nuclear Magnetic Resonance