Biophysical Chemistry

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.

Apply the theoretical models of molecular mechanics and molecular dynamics to study to biomolecular structure and function.

Describe in detail the theory and practice of physical methods such as chromatography, centrifugation, mass spectrometry and electrophoresis to examine biomolecular structure.

Describe classical theory and applications of spectroscopy to biomolecular structure, function and interactions (not limited to absorption, emission, and nuclear magnetic resonance spectroscopies).

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.

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.