CHEM 4450/5450 Biochemistry I

CHEM 4450/5450 is the first of a two-semester sequence in Biochemistry that is cross-listed as a graduate course. This course is taught in the fall and coincides with CHEM 4460, a one credit-hour laboratory course. The primary focus of this course is on biological macromolecules, namely proteins, nucleic acids and carbohydrates. The subject material loosely follows the organization of our reference Lehninger Principles of Biochemistry by Nelson and Cox, however the course is heavily dependent on group exercises and in-class work. The beginning of the course is spent reviewing organic and physical chemistry concepts essential to biochemistry. A thorough exploration of water molecules, their structure and hydrogen bonding follows before introduction to amino acids and proteins. Protein secondary, tertiary and quaternary structure will be examined to provide the foundation for studying enzymes in terms of their ligand/substrate specificity, catalytic rate enhancements, kinetics and allosteric regulation. The discussion of (deoxy)ribonucleic acids includes nucleotide and polynucleotide structure, basic nucleic acid chemistry, manipulations with molecular biology techniques, and biotechnological applications. Finally, carbohydrates (nomenclature, chemistry and diversity in nature), as well as lipids are covered.

CHEM 4470/5470 Biochemistry II

CHEM The second semester of the Biochemistry sequence focuses mainly on developing a foundation for a logical approach to understanding pathways and matabolism. For example, early learning goals include: recognizing evidence of participation of common cofactors and activated carrier molecules, functional group taxonomy to classify reactions with metabolites that might occur with coupling to ATP hydrolysis or ADP phosphorylation, cataloging the effects/involvement of network-level regulators such as cAMP-dependent protein kinase (PKA). These and other strategies are applied to learn core metabolic pathways including glycolysis/gluconeogenesis, TCA cycle, fatty acid catabolism, amino acid oxidation, lipid biosynthesis and amino acid/nucleotide biosynthesis. Finally, electron transport chains and hormonal regulation are addressed.

CHEM 4450/5450 Biochemistry I

CHEM 4460/5460 is the companion Biochemistry laboratory course. Standard biochemistry laborator concepts and techniques are covered. Recently, a research component has been integrated into the course in order to enhance student motivation and to strengthen skills in experimental design, data analysis, and communicating scientific results. The research component involves applying new skills related to protein purification, quantitation, biophysical analysis and characterization to research previously-unstudied proteins relevant to ongoing research at BGSU. A welcome outcome has been increased student participation in independent research outside of the course.

PCS 7040 Special Topics in Spectroscopy

This course is taken in the spring semester by second-year graduate students. The motivation for the course is to provide students with broad exposure to cutting-edge research and techniques related to photochemistry. This material is covered in approximately 1/3 of the semester. An important goal of this section of the course is to provide students with the skills to download and manipulate publicly-available macromolecular X-ray diffraction data. Students are given a review of protein structure and taxonomy followed by an introduction to the theory of X-ray diffraction and crystallography. Students are provided with electron density data and protein structures with deliberate errors in order to learn how to correct them using freely-available modeling and refinement software. The course material culminated with an exploration of the Photosystem II structure and time-resolvedprotein nanocrystallography experiments using theX-ray free-electron laser.