An analysis of the amide I mode in the vibrational spectra of unordered polypeptides and proteins | Zendy

Painter P. C. | Zendy; Coleman M. M. | Zendy

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An analysis of the amide I mode in the vibrational spectra of unordered polypeptides and proteins

Author(s) -

Painter P. C.,

Coleman M. M.

Publication year - 1978

Publication title -

biopolymers

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.556

H-Index - 125

eISSN - 1097-0282

pISSN - 0006-3525

DOI - 10.1002/bip.1978.360171014

Subject(s) - intramolecular force , amide , chemistry , dipole , raman spectroscopy , spectral line , sequence (biology) , crystallography , mode (computer interface) , coupling (piping) , rotational–vibrational coupling , stereochemistry , molecular physics , computational chemistry , chemical physics , infrared spectroscopy , physics , organic chemistry , quantum mechanics , materials science , biochemistry , computer science , metallurgy , operating system

The difference in the observed frequency of the amide I mode between the Raman and ir spectra of many unordered polypeptides is interpreted in terms of a model in which sequences of amide groups have similar ϕ, ψ angles. The splittings due to intramolecular interactions for the infinite helices generated by all ϕ, ψ angles are calculated by assuming transition dipole coupling. The effect of finite sequence length and distortions are then considered. This hypothesis accounts for the general features of the amide I mode of unordered polypeptides.

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