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Additional file 8: of Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

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posted on 2018-07-11, 05:00 authored by Santiago MartĂ­nez-Lumbreras, Ewelina Krysztofinska, Arjun Thapaliya, Alessandro Spilotros, Dijana Matak-Vinkovic, Enrico Salvadori, Peristera Roboti, Yvonne Nyathi, Janina Muench, Maxie Roessler, Dmitri Svergun, Stephen High, Rivka Isaacson
Figure S8. Mass spectrometry analysis of SGTA CT construct, showing that the protein is not covalently modified. Expected molecular weight = 10,877 Da. (PDF 2643 kb)

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    co-chaperone SGTAAdditionalsubstrate quality control Figure S 8. Mass spectrometry analysisPDF 2643 kbproteinDadimerizationSGTA CTC-terminal regioncovalentlyStructural complexity

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