Exam Format

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

• The mid-term will contain questions based on material covered in lectures only, whereas the final exam will contain questions on lecture (~75%) and laboratory work (~25%).

• Copies of last year's midterm and final examinations are included in the laboratory manual. Copies of other midterm and final examinations are available below and from the Science Students' Association :Online Examinations. 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 10 out of 15 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. See the staff in the Chemistry General Office, 360 Parker, to obtain a lab exemption. You are still responsible for the lab material on the final exam even if you have a deferral.

Continuation in CHEM 2780/MBIO 2780:

Final Exam Review:

Academic Dishonesty: Please visit the Faculty of Science web site Cheating, Plagiarism etc.

ATP

Lecture Schedule

N.B. The number of lectures indicated are only very approximate and are subject to change.

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).

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 5 & 6)

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 8)

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 (Chapter 9)

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 (Chapters 7 & 19)

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 10)

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. DNA METABOLISM (Chapter 20)

Replication, Meselson-Stahl experiment, molecular mechanism

DNA damage and its repair (thymine dimers)

11. RNA METABOLISM (Chapter 21)

RNA polymerase -- promoters etc.

RNA processing -- brief

RNA replicase and reverse transcriptase

12. PROTEIN METABOLISM (Chapter 22)

Introduction -- the problem, coding, "bilingual" tRNA

Genetic code

Mechanism of translation -- initiation, elongation, termination

Post-translational modification

Oleic Acid

Useful WWW Sites for CHEM 2770:

On-line Medical Dictionary

On-line Webster Dictionary

Metabolic Pathways of Biochemistry

The Main Metabolic Pathways on Internet

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