pone.0270572.s004.pdf (70.48 kB)
Download fileThe RMSD values of PRC-DD solution and crystal structures under different alignment conditions.
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posted on 05.08.2022, 20:04 authored by Fei Tan, Jin Xu(a) aligning a single monomeric unit. (b) aligning the whole homodimeric structures of PRC1-DD. (c) aligning a single monomeric unit in the homodimer. Residue number 1–67 denote the first monomeric unit, while 67–134 denote the second monomeric unit.
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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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