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Download fileFluorescence thermal shift assay of PRC1-DD and its mutants (bar graph representation of data in Table 2).
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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-DD 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 respective mutants’s colors are as labeled. Graphs were produced in MATLAB, plotted from the mean and standard deviations (thin red T) of Tm from four parallel experiments; 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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