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- W2050891454 abstract "Models of the helical portions of wool α-keratin sequenced by Crewther et al. (1976) show that they build well into a parallel two-stranded rope but three chains are unlikely to fit into any three-stranded rope. The 9.5-residue periodic pattern in the charged residues discovered by Parry et al. (1977) has been analysed further, suggesting that 9.5 rather than 28 residues is the fundamental period. The positively charged amino acids segregate into 11 zones, 3.5 residues wide and 9.5 residues apart. Possible structures for clusters of two-stranded coils are considered but none appear able to account for a strong 9.5-residue period. Instead it is probable that the pattern is related to a periodic interaction between the helical and non-helical portions of α-keratin." @default.
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- W2050891454 date "1978-09-01" @default.
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- W2050891454 title "Coiled coil formation and sequence regularities in the helical regions of α-keratin" @default.
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- W2050891454 doi "https://doi.org/10.1016/0022-2836(78)90163-8" @default.
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