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Proceedings Paper

Problems And Caveats Associated With The Determination Of Protein Conformation By FT-IR Spectroscopy
Author(s): H. H. Mantsch; W. K. Surewicz; A. Muga; D J Moffatt; H L. Casal
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Paper Abstract

Infrared spectroscopy is being used increasingly to study the conformational structure of proteins and polypeptides in aqueous solution. The methodology generally used for the infrared spectroscopic analysis of protein secondary structure is based on three steps: 1. Separation of the overlapping amide I (amide C = O stretching) component bands via band-narrowing procedures such as Fourier self-deconvolution or derivation. 2. Assignment of the resolved component bands, based on previously established spectra-structure correlations, to different secondary structure elements, i.e., alpha helices, beta-sheets, turns or non-ordered conformations. 3. Extraction of quantitative information on protein secondary structure from analysis of amide I band profiles by curve fitting. Each of these three steps has potential sources of error which have to be recognized to prevent fallacious interpretations.

Paper Details

Date Published: 1 December 1989
PDF: 2 pages
Proc. SPIE 1145, 7th Intl Conf on Fourier Transform Spectroscopy, (1 December 1989); doi: 10.1117/12.969611
Show Author Affiliations
H. H. Mantsch, National Research Council of Canada (Canada)
W. K. Surewicz, National Research Council of Canada (Canada)
A. Muga, National Research Council of Canada (Canada)
D J Moffatt, National Research Council of Canada (Canada)
H L. Casal, National Research Council of Canada (Canada)

Published in SPIE Proceedings Vol. 1145:
7th Intl Conf on Fourier Transform Spectroscopy
David G. Cameron, Editor(s)

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