Protein secondary structure from FT-IR spectroscopy : correlation with dihedral angles from three-dimensional Ramachandran plots

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DOIResolve DOI: http://doi.org/10.1139/v91-240
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TypeArticle
Journal titleCanadian Journal of Chemistry
ISSN0008-4042
1480-3291
Volume69
Issue11
Pages16391642
SubjectFT-IR spectroscopy; proteins; structure; dihedral angles
AbstractThe frequency of the so-called "amide I" band (amide C=O stretching vibration, vC=O) of proteins is discussed in terms of the dihedral angles of the various secondary structures present within proteins. We propose that in the case of intra- or intermolecular hydrogen-bonded amide carbonyl groups the frequency of this absorption can be directly related to the Φ, Ψ angles of the amide moieties for the major secondary structures. Amide 1 bands at frequencies above those found for non-hydrogen bonded amide carbonyl groups are rationalized in terms of a change in the third dihedral angle, ω. Rotation around the arnide C-N bond in sterically demanding structures, such as turns where ω deviates from 180°, is expected to cause an increase in the electron density of the amide carbonyl groups and so increase vC=O to frequencies greater than that seen for unperturbed carbonyl groups.
Publication date
LanguageEnglish
AffiliationNRC Steacie Institute for Molecular Sciences; National Research Council Canada
Peer reviewedYes
NPARC number23001389
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Record identifiere7c8923b-644b-4a78-b258-b5396abecdc0
Record created2017-02-01
Record modified2017-02-01
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