Fig. 3
From: The C-terminal domain of TPX2 is made of alpha-helical tandem repeats
Biochemical and structural analysis of TPX2. a SDS-PAGE analysis of Xenopus and Arabidopsis TPX2 proteins. b Spectra in the region of 260–190 nm were obtained at 25 °C for full length xlTPX2 and atTPX2. Both spectra present a typical alpha helical profile with two minima (λ208 and λ222 nm). c Molecular model of xlTPX2 (Q191-K715) represent a compact structure of repeated α-helices linked by a flexible loop. d Ramachandran plot of the xlTPX2 model. About 96 % of all residues were in favored regions, and about 4 % of the residues were in an allowed region. Two outliers were found, Leucines at positions 173 and 302, although, visual inspection did not reveal any steric clash