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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The secondary structure of myelin P2 protein derived by secondary structure prediction methods, circular dichroism, and 400-MHz 1H-NMR spectroscopy: implications for tertiary structure.

The various methods used to study the secondary and tertiary structure of myelin P2 protein, and one of its peptides (CN1), in aqueous solution, indicate that the native protein contains a significant fraction of alpha-helix, suggesting that the current prediction of an all-beta tertiary structure requires revision.[1]


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