Midterm and Exam Tutoring Sessions.
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See ONLINE Tutoring Session Details for lesson breakdown
The following sessions will be held online and recommended for student with: Dr. Shuhendler, Dr. Musgaard and Dr. FX
- 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
- 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
FULL Exam Review
- 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
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!