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The 18.5 kDa isoform of myelin basic protein (MBP) is a major component of the myelin sheath in the central nervous system of higher vertebrates, and a member of a larger family of proteins with a multiplicity of forms and post-translational modifications (PTMs). The 18.5 kDa protein is the exemplar of the family, being most abundant in adult myelin, and thus the most-studied. It is peripherally membrane-associated,...
The 18.5kDa isoform of myelin basic protein (MBP) has strong and probably specific interactions with phosphoinositides that are of interest regarding this protein's function, and in effecting its two-dimensional crystallization for structural determination. We have designed and constructed truncation mutants of recombinant 18.5kDa murine myelin basic protein (rmMBP) lacking either the N- or C-terminal...
The phosphoenolpyruvate synthase (EC 2.7.9.2) of the hyperthermophilic archaeonStaphylothermus marinus forms an unusually large (2.25 MDa) homomultimeric complex of 24 94 kDa subunits. This assembly stands in contrast with the more usual dimeric or tetrameric quaternary arrangements of phosphoenolpyruvate utilising enzymes from eukaryotes and eubacteria. Here, computerised image analysis and reconstruction...
The structure of the small ribosomal subunit of the mildly thermophilic fungus Thermomyces lanuginosus was reconstructed using spectroscopic electron microscopy and quaternion-assisted angular reconstitution to a resolution of roughly 3.3 nm. The distribution of phosphorus within this complex was also reconstructed and represents the arrangement of the phosphate backbone of the constituent ribosomal...
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