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CHEM 482. Biophysical Chemistry

Credits: 4
Department: Chemistry
Description: Biomolecular structure, thermodynamics and kinetics, and their study through spectroscopic techniques.
Prerequisites: CHEM 480, MATH 212 or MATH 222, PHYS 232 or PHYS 235
Semester Offered: Spring
Grading Method: ABCDF
Lab: Lab
Additional Information: Laboratory Rm located in WSB Addition

Student Learning Outcomes

1. Identify fundamental thermodynamic state functions, e.g., free energy, and apply this knowledge to analyze chemical and physical equilibria in biological systems, e.g., the protein folding and ligand-binding.
2. Apply the theoretical models of molecular mechanics and molecular dynamics to study to biomolecular structure and function.
3. Describe in detail the theory and practice of physical methods such as chromatography, centrifugation, mass spectrometry and electrophoresis to examine biomolecular structure.
4. Describe classical theory and applications of spectroscopy to biomolecular structure, function and interactions (not limited to absorption, emission, and nuclear magnetic resonance spectroscopies).
5. Use appropriate methodologies to crystalize biological molecules, and apply theory and concepts of Bragg+s Law and the von Laue conditions of x+ray diffraction to macromolecular crystal structure.
6. Develop critical thinking, problem solving and communication skills in relation to the physical and quantitative treatment of biomolecular structure via the review and critique of primary literature on the subjects of protein folding thermodynamics and kinetics, protein engineering and biomolecular design.






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