31 January 1994 Infrared investigation on the conformation of proteins deposited on polyethylene films
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Proceedings Volume 2089, 9th International Conference on Fourier Transform Spectroscopy; (1994) https://doi.org/10.1117/12.166695
Event: Fourier Transform Spectroscopy: Ninth International Conference, 1993, Calgary, Canada
Abstract
Aqueous protein solutions deposited and dried on thin polyethylene sheets were analyzed by Fourier transform infrared spectroscopy. This convenient technique provided reasonable determinations of secondary structure with 200 to 80 (mu) g of protein deposited. To determine secondary structure, principal component regression (PCR) was applied to the infrared spectra of 12 different proteins deposited as thin films. Regression with 5 principal components provided the fraction of helix and (beta) -sheet structure present in the hydrated proteins with standard deviations of 6.3% and 7.3%, respectively, compared to a reference data set of structures determined by x-ray crystallography. Prediction errors were similar to those obtained by other infrared methods. Analysis of various types of turn structure grouped together was unsuccessful.
© (1994) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Ronald W. Sarver, William C. Krueger, "Infrared investigation on the conformation of proteins deposited on polyethylene films", Proc. SPIE 2089, 9th International Conference on Fourier Transform Spectroscopy, (31 January 1994); doi: 10.1117/12.166695; https://doi.org/10.1117/12.166695
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