CHEMISTRY AND BIOCHEMISTRY 153A
WHAT YOU SHOULD KNOW FOR THE FINAL

The material covered in the last 2 weeks [i.e. TCA, through Oxidative Phosphorylation] will be emphasized slightly more heavily than the material on which you have already been tested. There will be emphasis on application of the general principals of metabolism and its regulation as illustrated by these pathways. For example, you will need to understand how the thermodynamics of metabolic reactions influence opposing pathways and their regulation. You need to know TCA at the same level of detail as glycolysis. However you should also be sure to review the earlier material as well. The exam will touch on nearly every topic covered in the course.

I. STRUCTURES

YOU SHOULD BE ABLE TO DRAW:

20 protein amino acids, peptide plates, peptide bonds, and peptide chains
straight chain and cyclic forms of glucose, mannose, galactose, fructose: sucrose, maltose,
glucopyranosides, cellobiose, cellulose, amylose, amylopectin, glycogen
fatty acids, glycerol, triacylglycerols, glycerophospholipids, micelles
metabolic intermediates of glycolysis and TCA cycle and glyoxylate bypass intermediates
"business end" of lipoamide (oxidized, reduced and acetylated)

YOU SHOULD BE ABLE TO RECOGNIZE:

secondary structures, supersecondary structures, acetals, hemiacetals, ketals, hemiketals, glycosides, ADP, ATP, Pi, NAD+, NADH, FAD, FADH2, TPP, CoA, Acetyl-CoA, biotin, heme, FMN, Fe-S clusters, CoQ, lipids, ethanolamine, choline, "fluid mosaic" membrane

II. COFACTORS & "CURRENCIES"

UNDERSTAND HOW THE FOLLOWING COMPOUNDS PARTICIPATE IN BIOCHEMICAL REACTIONS

ADP, ATP, Pi, NAD+, NADH, FAD, FADH2, TPP, CoA, Acetyl-CoA, biotin, FMN, Fe-S clusters, CoQ, heme (in Hb, Mb and cytochromes), lipoic acid, lipoamide

III. CONCEPTS

A. GENERAL

properties of water
acid/base chemistry: Henderson-Hasselbalch equation, titrations, buffering,
pKa's of protein amino acid sidechains
thermodynamics: concepts and equations related to Gibbs free energy and reduction potentials

B. PROTEINS

names, structure and properties of protein amino acids and polypeptides
know the approx. pKa's
formation of peptide bond
principals of peptide plate
levels of structural organization 1o,2o,3o,4o
protein folding: forces (covalent and weak interactions)
hemoglobin and myoglobin: structure and function, binding curves, heme, cooperativity
sequence determination: purposes of various reagents, specificities of proteases, solving sequences

C. CARBOHYDRATES

Fischer projections, Haworth projections
properties of sugars
structure and function
cyclization, mutarotation, reducing and non-reducting sugars
glycosides
nomenclature

D. LIPIDS

general properties, types of lipids and their functions, micelles, membranes limited nomenclature, including common and IUPAC names of fatty acids in the table of the compendium: same as midterm

E. ENZYME CATALYSIS

1. KINETICS

Michaelis-Menten equation: derivation, premises, calculations and graphing, meaning of Vo
Lineweaver-Burk, Eadie-Hofstee plots
effects of various types of inhibition on plots
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voh@chem.ucla.edu // Documents Processed: Wed June 10 10:11:42 PDT 1998