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- W3036435748 abstract "The technique of negative staining has been of very great value for directly determining the quaternary structure of individual multimeric proteins and viruses. In this regard, the iron-storage protein,, ferritin, is a notable exception for not having had its subunits unambiguously resolved by negative staining. Each ferritin molecule (d= 120Å) has an outer shell of 24 protein subunits (MW= 18,500) surrounding a variable amount of mineralized iron; published x-ray diffraction studies have not yet defined individual monomers in the polymeric shell. Claims that single subunits have been visualized in ferritin by electron microscopy (e.g.,6) all appear to be of highly doubtful validity since the phase granularity of the dried stain and supporting film has the same dimension as the presumed subunits; apparent subunits are readily visualized in defocused images, but are no longer discernable when brought closer to exact focus." @default.
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- W3036435748 date "1978-08-01" @default.
- W3036435748 modified "2023-09-25" @default.
- W3036435748 title "The resolution of individual protein subunits in ferritin" @default.
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- W3036435748 doi "https://doi.org/10.1017/s0424820100081772" @default.
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