Protein Structure By FTIR Self-Deconvolution

D. Michael Byler; Heino Susi

doi:10.1117/12.970815

20 December 1985 Protein Structure By FTIR Self-Deconvolution

D. Michael Byler, Heino Susi

Proceedings Volume 0553, Fourier and Computerized Infrared Spectroscopy; (1985) https://doi.org/10.1117/12.970815
Event: 1985 International Conference on Fourier and Computerized Infrared Spectroscopy, 1985, Ottawa, Canada

Abstract

Fourier self-deconvolution was applied to the peptide-carbonyl stretching vibration (amide I mode) of more than 20 globular proteins in deuterium oxide solution. This band, which usually exhibits little discernible fine structure, was thereby resolved into three to nine components. The individual components were assigned to protein segments consisting of extended chains, helices, and various turns and bends. The areas of the components were evaluated by Gauss-Newton iterative curve fitting with the assumption of Gaussian band shapes. Quantitative estimations regarding secondary structure were made by calculating the sum of the areas of the components asssociated with a particular conformation as a fraction of the total amide I band area. The results for helix content and for extended chain content are in good agreement with literature values obtained from X-ray data.

Citation Download Citation

D. Michael Byler and Heino Susi "Protein Structure By FTIR Self-Deconvolution", Proc. SPIE 0553, Fourier and Computerized Infrared Spectroscopy, (20 December 1985); https://doi.org/10.1117/12.970815

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