PMID: 9184943Apr 1, 1997Paper

Secondary structure of T4 gene 33 protein. Fourier transform infrared and circular dichroic spectroscopic studies

International Journal of Biological Macromolecules
W ShaoG M Sanders

Abstract

The secondary structure of bacteriophage T4 gene 33 protein (gp33) has been quantitatively examined by using Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy. Resolution enhancement techniques, including Fourier deconvolution and derivative spectroscopy were used to quantitate the spectral information from the amide I bands. The relative areas of these component bands indicate 21% alpha-helix, 25% beta-sheet, 34% turn, 12% random coil and 8% other undefined structures in gp33. An analysis of the CD spectrum of gp33 at the same pH and temperature revealed 19% alpha-helix, 25% beta-sheet, 13% turn and 43% random coil structures. The possible reasons for the discrepancies in estimates of the contributions to the secondary structure from turns and random coils are discussed.

Citations

May 12, 2004·Biochimica Et Biophysica Acta·F Javier MorenoE N Clare Mills
Sep 11, 2002·Journal of Molecular Biology·Scott E KoleskyE Peter Geiduschek
Dec 3, 2004·Proceedings of the National Academy of Sciences of the United States of America·Sergei NechaevE Peter Geiduschek

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