4.8 Editorial Material

Response to Comment on Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water

期刊

SCIENCE
卷 361, 期 6405, 页码 -

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AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar7949

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资金

  1. NIH [GM055694, GM097573, GM103622, 1S10OD018090-01, T32 EB009412, T32 GM007183, T32 GM008720]
  2. NSF [GRF DGE-1144082, MCB 1516959]
  3. U.S. Department of Energy [DE-AC02-06CH11357]

向作者/读者索取更多资源

Best et al. claim that we provide no convincing basis to assert that a discrepancy remains between FRETand SAXS results on the dimensions of disordered proteins under physiological conditions. We maintain that a clear discrepancy is apparent in our and other recent publications, including results shown in the Best et al. comment. A plausible origin is fluorophore interactions in FRET experiments.

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