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Since this protein was shown to contain high levels of ordered secondary structure (49% -helical structure, 17% -structure, and 34% random coil structure) it was pointed out that clathrin, being characterized by a very large frictional ratio, cannot represent a random coil polypeptide chain, and it was therefore hypothesized that this protein consisted of several globular (likely -helical) domains connected by flexible polypeptide sequences to form a common locus (Pretorius et al., 1981)

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doi:10.1016/j.chom.2013.04.010 [53] Cronin SJF, Woolf CJ, Weiss G, Penninger JM

(2014) 2014:CD008990

Jan 2010;24 Suppl 1:S20-8