BCH 2333/2733
Final Exam and Midterm Tutoring Sessions.
Book your sessions.
online learning
$40
3+ Hours of Tutoring
Cumulative Exam Review
(Problem Solving)
Review 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

Additional information
Date | April 19, 2022 5:00 PM to 8:30 PM (Live Zoom), Buy Review Session Recording |
---|
Content missing
Related products
$40
3+ Hours of Tutoring
Protein Binding and
Michaelis-Menten Kinetics
Review 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

Related products
$40
3+ Hours of Tutoring
Enzyme Inhibition,
Catalysis and Regulation
Review 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

Related products
$40
6+ Hours of Tutoring
Amino acids, Nucleotides
and Carbohydrates
Review Session Details
- Review Session will include tutoring with problem solving from past Midterms/Tests
- Understand how to assess amino acid stereochemistry
- Switch between line structure and Fisher projection for amino acids
- 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
- Composition of DNA and RNA nucleic acids
- 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)
- Drawing oligomers of DNA and RNA
- Mechanism for the formation of a phosphodiester bond
- Identifying nucleic acid base pairing and tautomers

Related products
$40
3+ Hours of Tutoring
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

Related products
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!