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Slices from three-dimensional 1H-13C NOESY-HSQC spectrum of PRC1-DD, that show characteristic cross-peaks from residues that possess distinctive conformations in solution and crystal structures.

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posted on 05.08.2022, 20:04 authored by Fei Tan, Jin Xu

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Validation of the solution structure of dimerization domain of PRC1
PLOS ONEPLOS ONE

Categories

  • Biophysics
  • Biochemistry
  • Physical Sciences not elsewhere classified
  • Cell Biology
  • Chemical Sciences not elsewhere classified
  • Cancer
  • Computational Biology

Keywords

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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