BCH 2333/2733 (Winter 2019)

BCH2333/2733 Midterm and Final Exam Review Sessions.

Your instructor is a Ph.D. graduate from the University of Ottawa specializing in Biochemistry. With expert guidance you will be able to tackle problems and be ready for your midterms or final exam. Complex concepts will be simplified. Gain the ability to apply theory to midterm/exam questions. You will learn how to approach problems through the eyes of an expert and you will become an expert yourself!

Session Instructor
ABDULLAH AKBAR, PHD
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Final Exam

$25

for 4-Hours

Cumulative Review Session

Tutoring Session Details
  • This review session will analyse and solve midterm/problem set questions and how to approach them from the topics below. Other questions and topics can be discussed during the session as well!

 

  • Peptide overall charge, isoelectric point (pI), H-H equation, buffer/titrations
  • Drawing peptide with proline/D-amino acids
  • Protein structure and folding
  • Protein digestion
  • Protein sequencing
  • Protein coopertivity and Enzyme Kinetics
  • Enzyme inhibition
  • Enzyme catalysis and regulation
  • DNA and RNA base pairs, nuclease cleavage, tautomers and acidity
  • Going from DNA code to peptide

Midterm 3

Please select the appropriate tutoring sessions for your course
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$35

for 3-Hours

Sugars
and Lipids

Review Session Details
  • Learn to sugar stereochemistry (i.e. D/L sugars, enantiomers, diastereomers, epimers)
  • Review structural difference between Ribose, Glucose, Mannose and Galactose and Fructose
  • Formation of hemi-acetals in cyclic and the concept of mutarotation about the anomeric carbon
  • Understand how to assess Fehlin's test
  • Learn to convert between Fisher projections, Haworth projection and line structures
  • Learn nomenclature for glycosidic bonds
  • Sugar function in a cellular context
  • Overview of lipid function in the cell and synthesis
  • Learn about fatty acid nomenclature, organization and properties
  • Key glycerophospholipid and sphingolipid structures
  • Understand the various properties of eukaryotic membranes (i.e. Mosaic model, membrane diffusion, lipid composition in outer/inner leaflet
  • Understand different protein interactions with lipid bilayer
  • Understand how cells facilitate diffusion across the lipid bilayer

BCH2333/2733-Midterm 3-Sugars and Lipids

$35.00

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CANCELLED

$35

for 3-Hours

Cooperativity and
Michaelis-Menten Kinetics

Tutoring Session Details
  • Understanding general ligand binding (i.e. formulate equation and associate it to Kd)
  • Learn to manipulate the simple Kd equation into complex ones
  • Graphically understand how protein-ligand system is interpreted
  • Cooperativity in ligand binding (i.e. Hill plot)
  • Assess the two types of cooperativity models (MWC vs. KNF model)
  • Apply protein-ligand cooperativity to oxygen transport in the body
  • Understand enzyme catalysis graphically and in-terms of Gibbs free energy
  • Understanding the Briggs-Haldane model and the steady-state approximation
  • Measuring the rate of enzymatic reactions with Michaelis-Menten enzyme kinetics
  • Understand the Michaelis-Menten equation
  • Graphically understand how to interpret Michaelis-Menten enzyme kinetics
  • Graphically understand the lineweaver-burke plot (double reciprocal of Michaelis-Menten graph)
  • Fully understand the following kinetic parameters: KM, Kd, kcat, kcat/KM

BCH2333/2733: Protein Binding and Michaelis-Menten Kinetics

$20.00

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$35

for 3-Hours

Enzyme Catalysis
and Inhibition

Tutoring Session Details
  • Understand general mechanism for enzyme catalysis (i.e. catalysis via induced fit, covalent catalysis, acid-base catalysis, catalysis by approximation and metal-ion catalysis)
  • Using specific case studies, learn to identify which type of catalysis is being used by enzyme
  • Learn how cofactors and coenzymes are involved in enzyme catalysis (with specific examples)
  • Understand how allosteric binding can lead to feedback activation or inhibition (will use Aspartate transcarbamoylase (ATCase) to understand concept)
  • Learn other forms of enzyme regulations such as: isozymes, reversible covalent modification, proteolytic cleavage and transcriptional control
  • Learn how various types of reversible inhibitors can affect Michaelis-Menten parameters (Km and Vamx)
  • Graphically understand how to determine which type of reversible inhibitor is present using a Line-weaver Burke plot
  • Learn about the different types of irreversible inhibitors

BCH2333/2733: Enzyme Catalysis, Regulation and Inhibition

$20.00

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Midterm 2

Divided into THREE review sessions
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$35

for 3-Hours

Protein Structure
and Folding

Review Session Details
  • Review amino acid side chain properties (i.e. pKa, charges, stereochemistry, trans/cis amide bonds)
  • Understand the 3 main dihedral angles regulating secondary structure (phi, psi and omega)
  • Apply dihedral angles to Ramachandran plot
  • Relate secondary structures to Ramachandran plot
  • Properties of helices (i.e. residues per turn, pitch, H-bonding, simple calculations, drawing helical wheel)
  • Properties of Beta-sheets (i.e. length per residue, H-bonding, types of turns, simple calculations)
  • Domains vs. motifs
  • How to identify type of quaternary structure (i.e. C2, C3, D2, D3 etc.)
  • Thermodynamics involved for protein folding
  • Understand what facilitates folding of proteins

BCH2333/2733: Protein Structure and Folding

$20.00

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$35

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DNA Structure
and Lipids

Review Session Details
  • Review primary DNA structure (i.e. base tautomerization, classic base pair H-bonding, c2/c3 endo sugar rings)
  • Understand the inter- and intramolecular interaction in a DNA double helix
  • Analyse and understand DNA secondary structures (i.e. DNA helices: A, B, and Z)
  • Remembering Chargaff's Rule
  • Understand properties of triple DNA helices (H-DNA)
  • Palindromes and formation of hairpins and
  • DNA denaturation and melting curves
  • Types of lipids and their structures
  • Lipid membrane properties (i.e. fluidity, lateral and transverse diffusion, and cholesterol)
  • Fatty acid nomenclature
  • Understanding general ligand binding (i.e. formulate equation and associate it to Kd)
  • Learn to manipulate the simple Kd equation into complex ones
  • Graphically understand how protein-ligand system is interpreted
  • Cooperativity in ligand binding (i.e. Hill plot)
  • Assess the two types of cooperativity models (MWC vs. KNF model)
  • Apply protein-ligand cooperativity to oxygen transport in the body

BCH2333/2733: DNA Structure, Lipids and Protein Binding

$40.00

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Session Recording – For Musgaard

$35

for 3-Hours

Enzyme Cooperativity
and Kinetics

Tutoring Session Details
  • Understanding general ligand binding (i.e. formulate equation and associate it to Kd)
  • Learn to manipulate the simple Kd equation into complex ones
  • Graphically understand how protein-ligand system is interpreted
  • Cooperativity in ligand binding (i.e. Hill plot)
  • Assess the two types of cooperativity models (MWC vs. KNF model)
  • Apply protein-ligand cooperativity to oxygen transport in the body
  • Understand the various ways an enzyme can catalyse a biochemical reaction
  • Measuring the rate of enzymatic reactions
  • Understand the Michaelis-Menten equation
  • Graphically understand how to interpret Michaelis-Menten enzyme kinetics
  • Graphically understand the lineweaver-burke plot (double reciprocal of Michaelis-Menten graph)
  • Fully understand the following kinetic parameters: KM, Kd, kcat, kcat/KM
  • Types of reversible inhibitors and how they affect enzyme kinetic parameters: KM and kcat

BCH2333/2733: Enzyme Kinetics and Inhibition

$40.00

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Date

Feb 26, 2020 at 5:00 PM to 9:30 PM

Midterm 1

Divided into THREE review sessions
To learn more click "review session details"

$35

for 3-Hours

Intermolecular Interactions, pH and Buffers

Review Session Details
  • Types of intermolecular interactions in biochemistry (i.e. ionic and dipole interactions)
  • Understand the hydrophobic effect
  • Understand the three thermodynamic parameters: ∆H, ∆S and ∆G
  • relate ∆G to equilibrium constants (Keq) of biochemical reactions
  • Acid dissociation in water and pKa
  • Learn to calculate for pH, pOH, pKa and pKb
  • Understand what is a buffer and its uses
  • Calculating pH for strong and weak acids/bases
  • Learn to comfortably draw titration curves for mono- di- and tri-protic acids
  • Understand how to use the Henderson-Hasselbalch equation appropriately
  • Learn to calculate amounts of solutes needed to make the appropriate buffer

BCH2333/2733: Thermodynamics and pH/Buffers

$20.00

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$35

for 3-Hours

Nucleotides, Amino Acids
and Peptides

Review Session Details
  • Composition and structure of DNA and RNA nucleic acids
  • Three conformations of nucleic acids
  • Comfortably draw oligomers of DNA and RNA
  • Learn the mechanism for the formation of a phosphodiester bond
  • Learn to identify nucleic acid base pairing and strand direction
  • Understand how to assess amino acid stereochemistry
  • Switch between line structure and Fisher projection for sugars
  • Learn the mechanism for the formation of a amide bond
  • Review 20 natural amino acids and their pKas
  • Amino acid charge at various pH and its isoelectric point (pI) values

BCH2333/2733: DNA/RNA Nucleotides and Amino Acids

$20.00

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$35

for 3-Hours

Thermodynamics
and Carbohydrates

Review Session Details
  • Types of intermolecular interactions in biochemistry (i.e. ionic and dipole interactions)
  • Understand the hydrophobic effect
  • Understand the three thermodynamic parameters: ∆H, ∆S and ∆G
  • relate ∆G to equilibrium constants of biochemical reactions
  • Formulate the appropriate ∆G equation at various conditions
  • Understand the free energy and spontaneity of biochemical reactions
  • Learn to predict equilibrium direction with using K, Q and ∆G
  • Many examples from midterms administered at uOttawa!

BCH2333/2733: Midterm 2 (Part 2 of 2)

$35.00

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Date

June 9, 2019 3:30 PM – 7:30 PM