Abstract
MT may be described as regular helical assemblies of two slightly elongated protein subunits, tubulins α and ², each of about 55,000 daltons molecular weight. The shape and properties of MT proceed from the linkages of these two closely related molecules. However, other proteins appear to be necessary for tubulin assembly into MT or may become closely linked with MT when these assemble into complex structures such as centrioles, basal bodies, cilia or axonemes (cf. Chap. 4). It is more and more evident that the tubulin subunits may assemble in more than one way, and tubulin “polymorph” have repeatedly been described, and help to understand the steps and the factors required for assembly. Tubulins are also associated with guanine nucleotides, possibly with enzymes and with non-protein components: the molecular structure of MT may thus be far more complex than a helical association of protein subunits.
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Dustin, P. (1978). Structure and Chemistry of Microtubules. In: Microtubules. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-96436-7_4
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