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Historical review: another 50th anniversary: new periodicities in coiled coils

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Gruber,  M
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Lupas,  AN       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Gruber, M., & Lupas, A. (2003). Historical review: another 50th anniversary: new periodicities in coiled coils. Trends in biochemical sciences, 28(12), 679-685. doi:10.1016/j.tibs.2003.10.008.


Cite as: https://hdl.handle.net/21.11116/0000-000B-60E1-A
Abstract
In 1953, Francis Crick and Linus Pauling both proposed models of supercoiled alpha helices ('coiled coils') for the structure of keratin. These were the first attempts at modelling the tertiary structure of a protein. Crick emphasized the packing mode of the side-chains ('knobs-into-holes'), which required a periodicity of seven residues over two helical turns (7/2) and a supercoil in the opposite sense of the constituent helices. By contrast, Pauling envisaged a broader set of periodicities (4/1, 7/2, 18/5, 15/4, 11/3) and supercoils of both senses. Crick's model became canonical and the 'heptad repeat' essentially synonymous with coiled coils, but 50 years later new crystal structures and protein sequences show that the less common periodicities envisaged by Pauling also occur in coiled coils, adding a variant packing mode ('knobs-to-knobs') to the standard model. Pauling's laboratory notebooks suggest that he searched unsuccessfully for this packing mode in 1953.