Potschka, Martin published the artcileThe two coiled coils in the isolated rod domain of the intermediate filament protein desmin are staggered. A hydrodynamic analysis of tetramers and dimers, Related Products of alcohols-buliding-blocks, the publication is European Journal of Biochemistry (1990), 190(3), 503-8, database is CAplus and MEDLINE.
Desmin protofilaments and the proteolytically derived α-helical rod domain have been characterized by high-resolution gel permeation chromatog. (GPC) using columns calibrated for the determination of viscosity radii. Addnl. characterization by chem. crosslinking and the determination of sedimentation values allowed the calculation of the mol. dimensions of the mol. species isolated. In dilute buffers GPC separated desmin rod preparations into 2 complexes: a dimer species (single coiled coil) with a length of 50 nm and a tetramer species (2 coiled coils) with a length of 65 nm. Thus the 2 coiled coils in the tetramer are staggered by ∼15 nm. The hydrodynamically derived lengths of the rod dimer and tetramer are supported by electron microscopy after metal shadowing. The hydrodynamic properties of desmin protofilaments follow that of the rod tetramer. The present results explain the inhomogeneity of mols. encountered in previous electron microscopical analyses.
European Journal of Biochemistry published new progress about 70539-42-3. 70539-42-3 belongs to alcohols-buliding-blocks, auxiliary class pyrrolidine,Ester,Amide,Inhibitor,Inhibitor, name is Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, and the molecular formula is C18H20N2O12, Related Products of alcohols-buliding-blocks.
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