Vibrational Circular Dichroism of Protein Films

Vibrational Circular Dichroism of Protein Films
Received March 23, 2004
Web Release Date: July 29, 2004
Ganesh Shanmugam and Prasad L. Polavarapu*
J. Am. Chem. Soc.
ACS Publications
Copyright © 2004 American Chemical Society
Contribution from the Department of Chemistry, Vanderbilt University, Nashville, Tennessee 37235
Vibrational circular dichroism (VCD) spectra in the 1800-1400 cm-1 region have been measured for the first time for protein films prepared from aqueous buffer solutions. These measurements demonstrate several advantages of significant importance. First, the interference from infrared absorption of water in the amide I region, which is a serious limitation for measurements in water solutions, is eliminated. Second, the amounts of protein samples required for VCD measurements on films are approximately 2 orders of magnitude smaller than those required for the same in water solutions. In addition, the amide I absorption and VCD bands of protein films are found to be independent of film orientation. Furthermore, characteristic VCD patterns have been observed for protein films whose secondary structure is dominated by -helix, -sheet, and + combinations. These results demonstrate that VCD can be used to study the structure of proteins in the film state.
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