CHEM 325 Biochemistry I: Biomolecule Structure and Function

General

• Generalize the concept of a titration to biochemical measurement
• Know how changes in pH, temperature, salt, and detergent influence protein stability
• Understand how enzyme activity is measured and the fundamentals of enzyme assays
• Know the mechanisms of enzyme inhibition and the differences between competitive, non-competitive, and uncompetitive inhibitors
• Describe the structure and properties of nucleotides and nucleic acids, taking advantage of insights provided by organic chemistry
• Know the structure and function or carbohydrates, lipids, and fatty acids
• Use insights from organic chemistry to describe protein structure, carbohydrate and nucleic acids, and how functional groups effect their chemical properties
• Recognize and use Michaelis-Menten kinetic scheme
• Know the chemical properties of the naturally occurring 20 amino acids
• Explain and sketch the periodic arrangements of secondary structures within a protein fold
• Understand the packing of secondary structures to form tertiary structures
• Use analysis of hydrophobic interactions and properties of water and how they influence protein folding in solution and in membranes
• Distinguish and explain negative and positive cooperativity and allosteric interactions
• Review the properties of buffers and the concept of pH and how solution pH influences protein stability and enzyme kinetics
• Know the basics of enzyme kinetics and, using simple examples, mathematically describe enzyme-catalyzed reactions and the derivation of their key constants