Vibrational analysis of peptides, polypeptides, and proteins. I. Polyglycine I

Authors

  • W. H. Moore,

    1. Harrison M. Randall Laboratory of Physics and Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Michigan 48109
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  • S. Krimm

    1. Harrison M. Randall Laboratory of Physics and Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Michigan 48109
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Abstract

A force field has been refined for the antiparallel chain-rippled sheet structure of polyglycine I. Transition dipole coupling and hydrogen bonding are explicitly taken into account. Amide I and amide II mode splittings are well accounted for, the latter also providing a quantitative explanation of the amide A and amide B mode frequencies and intensities. In addition to predicting other features of the vibrational spectrum of polyglycine I, this force field is completely transferable to other β polypeptides, even though these have the antiparallel chainpleated sheet structure.

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