| DOI | Resolve DOI: https://doi.org/10.1117/12.969611 |
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| Author | Search for: Mantsch, H. H.1; Search for: Surewicz, W. K.1; Search for: Muga, A.1; Search for: Moffatt, D. J.1; Search for: Casal, H. L.1 |
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| Affiliation | - National Research Council of Canada
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| Format | Text, Book Chapter |
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| Conference | 7th International Conference on Fourier Transform Spectroscopy, June 19, 1989, Fairfax, Virginia, USA |
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| 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. |
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| Publication date | 1989-12-01 |
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| Series | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 23001099 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 41f5648a-fc75-4cb5-b271-baa4fb547441 |
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| Record created | 2016-12-13 |
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| Record modified | 2020-06-10 |
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