Today’s topics : Review

1. Today’s topics: Review • Be able to classify amino acids as nonpolar, polar, acidic, or basic. (2) • Distinguish among saturated, monounsaturated, polyunsaturated, and trans fatty acid. (1) • Describe the structural features of triglycerides, phosphoglycerides, and steroids, and explain how these features relate to their function in the body. (3) • Be able to use the HenersonHasselbach equation as it applies to the ionization of carboxyl and amino groups of amino acids/proteins. Describe isoelectric point, pI. (2) • Be able to recognize and/or describe the structure of glucose, fructose, ribose, and glycogen. (1) • Describe the sequence of a protein. Describe the characteristics of the peptide bond that makes it planar and how this relates to f and y angles used to describe protein secondary structure. (2) • Describe the type of interaction that creates secondary structure. Describe the characteristics of the three types of secondary structure. (2)

2. Describe the 4 types of tertiary structure. Be able to predict what amino acids will tend to form each of these types of tertiary structure. (2) • Define quaternary structure. What type of interactions are involved? Distinguish between the functions of hemoglobin and myoglobin and how that relates to their quaternary structure. (2) • Be able to apply the equation, DG = DG + RT ln Q, to determine the direction of reactions. (1) • Describe the meaning of the equation DG = DH - T DS. How does it relate to protein folding and DNA ‘melting’. (1) • Describe the influence an enzyme has on DG, and Eact for a reaction. (2) • Describe the basic elements of enzyme nomenclature. Be able to apply this to explain the function of specific dehydrogenases and kinases. (1) • Describe the MichaelisMenten parameters, KM, Vmax. Explain how they are determined. Describe kcat. Explain the criteria to determine enzyme efficiency at low [S] and at high [S]. (3) • Describe an allosteric enzyme and explain how this aids in regulation of metabolism. (1)

3. Describe enzyme inhibition and distinguish between competitive and noncompetitive inhibition. (1) • Know the major reaction, purpose, location, and regulation (4 Ws) for : glycolysis, bridging reaction, Krebs cycle, oxidative phosphorylation, glycerol-phosphate shuttle, gluconeogenesis, glycogenesis, glycogenolysis, b-oxidation, fatty acid synthesis, ketogenesis, transamination, oxidative deamination, pentose phosphate pathway, transketolase/transaldolase. (11) • Describe the metabolic role of NADH, ATP, NADPH, Lactate dehydrogenase, phosphorylase, glycogen synthase, glucagon, insulin, leptin, epinephrine, ATP synthase, UCP, proton gradient, glycerol-phosphate dehydrogenase, glutamate dehydrogenase, glucose-6-phosphatase, acetylCoAcarboxylase, pyruvate carboxylase, phenylalanine hydroxylase, ubiquitin, and lipase. (2) • Distinguish between a-keto acids and amino acids; and glucogenic and ketogenic amino acids. (2) • Describe the metabolic deficiency in McArdle’s Disease, Von Gierke’s disease, diabetes, PKU, and Wernicke Korsakoff syndrome. (2) • Describe the composition of nucleosides and nucleotides. Know the base-pairing schemes for nucleotides (given their structures). Describe the influence that tautomerism has on base pairing and what are the consequences of this. (5)