Tuesday, October 16, 2018
Savannah J. West
Department of Chemistry
Mississippi State University
Location: HL 1144
Time: 4:00 PM
Circular dichroism (CD) spectroscopy has been used for decades to determine the structural characteristics of proteins. Light is circularly polarized by rotating the direction of the electric field vector around the direction of propagation. Different secondary structures of proteins (α-helices, β-sheets and turns, etc.) will absorb left and right-handed circularly polarized light to different degrees, providing qualitative information on the secondary structure of proteins. This technique has several shortcomings that can be alleviated by using synchrotron radiation as a beam source. Conventional circular dichroism spectroscopy is often unable to sufficiently determine the characteristics of proteins with mixed α-β characteristics, that are rich in β-sheets, or are disordered. Buffers which are commonly required for proteins to retain their secondary structure characteristics in solution will often absorb light in the near-UV wavelength range, where conventional CD spectroscopy generally has a very low intensity. Synchrotron radiation circular dichroism (SRCD) spectroscopy provides an extended wavelength range into the far-UV region that can provide additional information on protein structure and under more varying conditions. This seminar will discuss the use of SRCD spectroscopy to determine the structure of these proteins. Additionally, the determination of the tertiary and quaternary structures of proteins, ligand-protein binding interactions, and the preferred buffer conditions for protein analysis will also be discussed.
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