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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 isola ted 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 wel l 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 lev el 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&B 395 may also be taken in lieu of one (1) semester of Integrated Chemistry Laboratory (CHEM 375 or 376)
Unless preregistered students attend the first class meeting or communicate directly with the instructor prior to the first class, they will be dropped from the class list. NOTE: Students must still submit a completed Drop/Add form to the Registrar's Office.
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)
Last Updated on MAR-19-2002
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