Biochemistry (4650) Highlights of Key Points Keep in mind that you are expected to build on your knowledge and

not forget the information after an exam. Chapters 1,2,3,4, 5.1-5.3 (Exam 1) Cells and Thermodynamics
Know the generalized cellular structures and their functions in eukaryotic and prokaryotic cells. Know the 1st and 2nd laws of thermodynamics. Understand what is meant by enthalpy, entropy and Gibbs free energy and the equation relating them to each other. Know the equations relating G, Go, Keq, and product and reactant concentrations and be able to solve for any of the variables. Understand and know how to apply equilibrium constants, Le Chatliers Principle, coupled reactions (Hess Law), and know biochemical standard states and deviations from cellular conditions.

Water Thoroughly understand the chemical properties of water and its ability to act as a solvent. Know the properties of hydrogen bonds. Know what is meant by osmosis and the causes/effects of water movement. Thoroughly understand pH and the mechanism of buffers. (Know Henderson-Hasselbalch and that it derives from definition of KA). Know the significance of pKA, and relationship of pKA, pH and ionization. BE SURE YOU CAN EXPLAIN HYDROPHOBIC INTERACTIONS. Nucleotides/Nucleic Acids
Know the structures of the 5 standard nucleotide bases and be able to draw any nucleotide. Know the function of DNA, mRNA, tRNA and rRNA. Know the general structure of DNA and RNA, including base pairing. Understand why the products of ATP hydrolysis have lower energy than the reactants. Be aware that nucleotide structures are incorporated into molecules other than nucleic acids. Introduction to Protein Structure and Purification Know the structures of the 20 standard amino acids, their 3 letter code, the properties of their side chains, amino and carboxy termini, and determination of pI. Understand that there are other amino acids. Know the structure and properties of a peptide bond. Know the strategy and methods of protein purification and be able to apply the techniques to a mixture of proteins. (Solubility, column methods, electrophoresis, ultracentrifugation.) Understand the principles of ELISA. Know the principles of SDS-PAGE and isoelectric focusing and be able to apply them. Sequencing a protein: know the chemistry of Edman degradation and peptide hydrolysis into amino acids; understand cystine cleavage, and importance/reagents for cleavage of specific peptide bonds. Know the overview of the principles of protein sequencing using mass spectrometry.