Elastic Moduli of Helical Polypeptide Chain Structures.
The elastic moduli of the alpha-helix, polyglycine II, and the parallel-chain and antiparallel-chain pleated sheet structures have been calculated. A Urey-Bradley type of potential was used, extended by the inclusion of hydrogen bond stretching terms where appropriate. In the one instance where a valid comparison with experimental data can be made, viz, alpha-keratin, the calculations indicate that the matrix component, rather than being amorphous, probably contains an ordered structure of higher modulus than the alpha-helix.
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