BCH 2333/2733

BCH 2333/2733
Midterm and Exam Review Sessions.
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 online learning

Final Exam Review Session.

$40

for 4-Hours of tutoring

Cumulative Exam
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

BCH2333/2733-Cumulative Exam Review Session

$40.00

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Date

April 14, 2021 4:00 PM – 8:00 PM

Recordings of Review Sessions - DISCOUNTED PRICE

$20

for 4-Hours of tutoring

Thermodynamics and
pH/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

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DNA/RNA Nucleotides
and Amino acids

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

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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

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Protein Binding and
Michaelis-Menton 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

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Enzyme Catalysis,
Regulation 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

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Session Instructor
ABDULLAH AKBAR, PhD
Abdullah is a top-rated tutor with 7+ years of teaching experience.
­

­As a recent PhD graduate from the University of Ottawa, he has worked along with many of the CHM BCH 233/2733 Professors. His lesson plans will always begin with must-know fundamental concepts and end with examples from previous midterms and final exam questions.

Recommended by 200+ uOttawa students. Join one of his review sessions and decide for yourself!