Exam Format

• Both the mid-term and final exams will consist of machine-marked, multiple-choice questions.

• Copies of midterm and final examinations from previous years are available below. Working through them will help prepare you for the examinations.

Lab Exemptions:

If you have taken the course within the last two years and obtained a grade of 70% on the laboratory reports you are eligible for a lab exemption when repeating the course for the first time. The lab mark will be carried over. For all subsequent attampts the lab must also be repeated. To obtain a lab exemption please fill in and submit a lab-exemption request form: Lab Exemption Request Form. Note that if you VW the course you will not be eligible for a lab exemption.

Continuation in CHEM 2780/MBIO 2780:

Final Exam Review:

Academic Integrity: All faculty and students at the University of Manitoba are expected to act with academic integrity. For information on this topic please visit the Faculty of Science web site Cheating, Plagiarism etc. and read the appropriate sections of the Academic Calendar and pages 7-8 and the inside cover of the lab manual.

ATP

Lecture Schedule

1. INTRODUCTION AND TYPES OF BIOLOGICAL MOLECULES (Chapter 1).

Entropy, enthalpy, and free energy.

Equilibrium constants.

2. WATER -- ITS EFFECT ON BIOMOLECULES (Chapter 2)

Buffers. Ionization of H2O, pH, weak and strong acids and bases.

Titration curves and pKa values. Calculations of pH. Use of Henderson-Hasselbalch Equation in calculations and making buffer solutions. Carbonic acid/bicarbonate buffer in blood.

3. AMINO ACIDS (Chapter 3)

Structure and classification according to R group. Selected chemical properties.

Stereochemistry, chirality, D- and L-forms, biological importance of chirality.

Ionic properties and titration curves of amino acids. Isoelectric pH (pI).

4. PEPTIDES & PROTEINS (Chapters 4 & 5).

Introduction to peptide & protein structure

Working with proteins

Covalent (Primary) Structure -- sequence determination

Three-dimensional structure The peptide bond; secondary structure and the forces maintaining it exemplified by the alpha-helix and beta-sheet .

Tertiary & quaternary structures and the forces maintaining them exemplified by globular and fibrous proteins.

Denaturation by heat, pH changes etc.

5. ENZYMES (Chapters 6-8)

General properties and classification.

Enzymes as catalysts -- the active or catalytic site, activation energy and reaction rates.

Enzyme kinetics: reaction rates, effects of enzyme concentration, pH, temperature, and substrate concentration. Michaelis-Menten equation, significance of Km and Vmax. Lineweaver-Burk (reciprocal) plots. Enzyme specificity.

How enzymes increase reaction rates: proximity and orientation effects, bond-stress, catalytic

R-groups and role of metal ions.

Enzyme inhibition: Reversible inhibition -- competitive and non-competitive inhibition. Irreversible inhibition.

Enzyme regulation: allosteric effects, feed-back inhibitors, activators. Sigmoidal kinetics. Regulation via covalent modification.

6. CARBOHYDRATES (Chapter 10)

Monosaccharides: Aldose and ketose nomenclature, stereochemistry, D-

and L-classification, enantiomers and epimers. Intramolecular hemiacetal

and hemiketal formations. Anomers. Mutarotation.

Sugar derivatives, glycosides.

Disaccharides: maltose, isomaltose, lactose, sucrose.

Reducing and non-reducing sugars.

Polysaccharides: Starch, glycogen, chitin and cellulose.

7. LIPIDS & MEMBRANES (Chapters 11 & 12)

Classification of lipids.

Structure & properties of fatty acids.

Structure & properties of triacylglycerols (fats and oils), waxes.

Membrane lipids: glycerophospholipids, sphingolipids (glycosphingolipids and gangliosides). Sterols and steroids, e.g. Cholesterol.

Amphipathic nature of membrane lipids.

Membranes: Composition. The Fluid-Mosaic model: bilayers, integral and perip heral proteins,

control of membrane fluidity through changes in fatty acid composition.

Asymmetric nature of membrane surfaces. Selectedunctions of membranes.

8. NUCLEOTIDES and NUCLEIC ACIDS (Chapter 33)

Purines and pyrimidines. Nucleosides, nucleotides. Ribo- and deoxyribonucleotides.

Polynucleotides and nucleic acids. RNA and DNA.

Structure of DNA: Chargaff’s rules, base pairing, the right-handed double-helical DNA and the forces stabilizing it. Some properties of DNA.

9. BIOENERGETICS (Chapter 15)

Spontaneous and non-spontaneous processes. Endergonic and exergonic processes. Standard free energy changes and equilibrium constants. Oxidation reduction reactions and reduction potential. Biological electron carriers.

ATP structure and properties as a "high-energy" phosphate. Low-energy phosphates. Free energies of hydrolysis as measure of phosphate transfer potentials. Other "high-energy" compounds.

Use of ATP in driving unfavorable reactions.

10. ATP PRODUCING PATHWAYS (Chapters 16 and 18-21)

Direct production via substrate level phosphorylation exemplified by anaerobic prpcesses (glycolysis, alcoholic fermentation) (Ch 16).

Indirect production involving aerobic degradation of glucose (and other foodstuffs) via acetyl-S-Coenzyme A: the TCA Cycle (Ch 18 & 19).

Electron transport and oxidative phosphorylation: Components and energetics of the electron-transport chain. Chemiosmotic theory & ATP yield (Ch 20 & 21).

Oleic Acid

Useful WWW Sites for CHEM 2770:

On-line Medical Dictionary

On-line Webster Dictionary

KEGG Metabolic Pathways

Cells Alive!

National Human Genome Research Institute

Material Safety Data Sheets

Return to the Chemistry Department Course Descriptions

Return to Joe O'Neil's Home Page

http://home.cc.umanitoba.ca/~joneil/CHEM2770.Course.outline.htm

Maintained by J. O'Neil