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Proceedings Paper

Infrared investigation on the conformation of proteins deposited on polyethylene films
Author(s): Ronald W. Sarver; William C. Krueger
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Paper 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.

Paper Details

Date Published: 31 January 1994
PDF: 2 pages
Proc. SPIE 2089, 9th International Conference on Fourier Transform Spectroscopy, (31 January 1994); doi: 10.1117/12.166695
Show Author Affiliations
Ronald W. Sarver, Upjohn Co. (United States)
William C. Krueger, Upjohn Co. (United States)


Published in SPIE Proceedings Vol. 2089:
9th International Conference on Fourier Transform Spectroscopy
John E. Bertie; Hal Wieser, Editor(s)

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