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Chemically microtubules are class of fibrous proteins formed within a cell. These long, linear, and stiff polymers abound throughout the cytoplasm and are the governing structures that control the organization and function of membrane-bound organelles and other relevant components within the cell.


Following synthesis and during activity, there are molecular rearrangements within these microtubules are stabilized with accessory proteins, which are specific for particular tubulin (Alberts et al., 2008). In this assignment from different cellular examples, these interactions between the specific accessory proteins and the microtubule molecular structure will be examined in order to describe the structures and functions of these specific accessory proteins.
While these filaments abound in the cytosol of the eukaryotic cells, they have been classified into three categories based on size indicated by their diameter, type of the subunit, and subunit arrangement. The smallest of them are actin filaments which have a twisted double-stranded structure of 8 to 9 nm. The largest are microtubules which are essentially hollow tubes of adjacent protofilaments of 24 nm. The intermediate filaments are 10 nm in diameter. While each type of these cytoskeletal filaments is a polymer of protein subunits, the monomeric actin subunits assemble into microfilaments, which have dimeric subunits composed of alpha and beta tubulins that polymerize into microtubules (Alberts et al., 2008). ...
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