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Download fileResults from fluorescence thermal shift assay (FTSA) of PRC1 1–486 and its mutants (bar graph representation of data in Table 3).
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posted on 05.08.2022, 20:04 authored by Fei Tan, Jin Xu(a) Bar graph showing the mid-denaturation temperature (Tm) of wild-type PRC1 1–486 and its mutants. The name of each mutant is labeled on the x-axis of the figure, R2M refers to Δ1R2M. (b) Changes in Tm (ΔTm) of mutants compared with wild type. The mutants are color-coded according to the figure legend. Graphs were produced in MATLAB; the mean and standard deviation of Tm were calculated from four parallel runs of each experiment. single star indicates statistical significance (p<0.05) and double star indicates strong significance (p<0.01).
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hydrophobic core packingdeuterium exchange experiments>- helix h2proteins called microtubulecycle dependent proteinsn terminal residuesalso generated mutantsdiv >< pconformation prc1 adoptedhigh resolution threeprc1 </ presolution solution structureassociated proteinsn terminusalso differentalpha </prc1 ’prc1 callswhole proteinused hydrogenthermal stabilityspindle midbodysolution structuressolution structureresults suggestplacing hurdlesphysiological significancenmr spectroscopyincomplete sidechainshuman mapfunction relationshipsdistinguishing memberdimerization domaindimensional structurebind microtubules
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