AVS 56th International Symposium & Exhibition
    Biomaterial Interfaces Thursday Sessions
       Session BI-ThP

Paper BI-ThP14
Temperature-Induced Conformational Changes of Antifreeze Proteins in Aqueous Solution via Overlayer-Enhanced Attentuated Total Reflectance Fourier Transform Infrared Spectroscopy (OE-ATR-FTIR)

Thursday, November 12, 2009, 6:00 pm, Room Hall 3

Session: Biomaterial Interfaces Poster Session II (Arrays, Sensing, Micro/Nanofabrication, SPM)
Presenter: T. Ng, University of California, Davis
Authors: T. Ng, University of California, Davis
D.P. Land, University of California, Davis
X. Wen, California State University, Los Angeles
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Protein structural studies are commonly performed using techniques such as X-ray diffraction and Nuclear Magnetic Resonance (NMR). Unfortunately, these techniques make it difficult to study proteins in their native environment. Studies on protein structures via FTIR are often done with high protein concentration or in deuterated solvent. Tethering a protein near the interface of a gold-coated germanium internal reflection element (IRE) concentrates the protein near the interface and allows one to detect the protein with an increased signal-to-noise. By analyzing the amide I spectral region of the protein, the secondary structure of the protein can be determined and any conformational changes in these structures can be monitored. The secondary structure of an antifreeze protein extracted from Dendroides canadensis is determined in the aqueous and frozen states and show a decrease in the amount of beta sheet structures and an increase in the amount of turn structures upon freezing.