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One of the major catalysts of the revolution in biology that is now under way is our current ability to determine the physical properties and three-dimensional structures of biological molecules by x-ray diffraction, nuclear magnetic resonance spectroscopy and other spectroscopic methods. This course is designed to familiarize students with current research techniques in biochemistry and molecular biophysics. Students will perform spectroscopic investigations on a protein that they have isolated and characterized using typical biochemical techniques, such as electrophoresis, enzyme extraction and column chromatography. It will provide hands-on experience with spectroscopic methods such as NMR, fluorescence, UV-Vis absorption and Raman as well as bioinformatic computational methods. All these methods will be applied to the study of biomolecular structure and energetics. This course provides a broad knowledge of laboratory techniques valuable for independent research at the undergraduate level and beyond. This course can be taken in lieu of MB&B294 to satisfy the MB&B major upper-level laboratory requirement. For biological chemistry majors, MB&B395 may also be taken in lieu of one (1) semester of Integrated Chemistry Laboratory (CHEM375 or 376).
COURSE FORMAT: Laboratory
Level: UGRD Credit: 1 Gen Ed Area Dept: NONE Grading Mode: Graded
Prerequisites: (MB&B208 AND CHEM141 AND CHEM142) OR (MB&B208 AND CHEM143 AND CHEM144) Links to Web Resources For This Course.
Last Updated on MAR-30-2006
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