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B. Sc. Biochemistry & Molecular Biology
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Selected tags:
#enzyme
Account for why a given ligand may be bound tightly by an enzyme or covalently modify an enzyme (transition state analogues).
[
BIOC 4701
]
Distinguish between receptor/non-receptor kinases.
[
BIOC 4305
]
Explain how enzymes can increase the rates of biochemical reactions at the molecular level, and how they may be inhibited or regulated by drugs and toxins.
[
multiple courses
]
Explain how given techniques (spectroscopy, radioactivity, HPLC) may be used to measure enzyme activity in direct or indirect assays.
[
BIOC 4701
]
Given a pH-dependent kinetic mechanism, derive an initial velocity equation and sketch the plot of kinetic constants as a function of pH.
[
BIOC 4701
]
Given the architecture of an enzyme active site, write a mechanism and show how general acid/base, covalent, or electrophilic catalysis may occur.
[
BIOC 3700
]
Given the kinetic mechanism (with or without inhibition), derive an initial velocity equation using either the steady-state assumption or the rapid equilibrium approach.
[
multiple courses
]
Identify how post-translational modifications modulate the biophysical and the chemical properties of amino acid side chains to expand the functionality of proteins, particularly enzymes.
[
BIOC 4700
]
Interpret given diagrams of enzyme regulation/activity.
[
BIOC 2300
]
Recognize GTPases as on/off switches in vesicular transport and cellular signaling.
[
BIOC 3300
]
Show how entropic contributions lead to huge intramolecular rate enhancements.
[
BIOC 4701
]
Determine the effects of loss of function or gain of function mutations of regulating enzymes or metabolic enzymes on the rate of a reaction given a schematic of enzyme regulation.
[
BIOC 2300
]
Given the kinetic parameters for an enzyme-catalyzed reaction and the corresponding nonenzymatic reaction, calculate the efficiency, rate enhancement, proficiency, and extent of transition state stabilization.
[
BIOC 4701
]
Given the steady-state velocity expression for a multisubstrate enzyme, predict the product inhibition pattern and binding order in the presence of fixed and variable substrate concentrations.
[
BIOC 4701
]
Recall the activity of the main vitamin classes and their association with enzyme as cofactors.
[
BIOC 2300
]
Derive the steady-state velocity equation for a given kinetic mechanism for a multisubstrate enzyme using the King-Altman method.
[
BIOC 4701
]
Given the substrates, products, and cofactors for a particular class of enzyme-catalyzed reaction, write a mechanism for the reaction.
[
BIOC 3700
]
Identify uniform and differential binding from site-directed mutagenesis studies or substrate mutilation studies to discern the role of residues in transition state and ground state binding.
[
BIOC 4701
]
Recall the steps of glucose metabolism, citric acid cycle, fatty acid metabolism, amino acid metabolism; identifying the intermediates, enzymes, and regulatory steps.
[
BIOC 2300
]
Given an enzyme mechanism, design a reversible or irreversible inhibitor.
[
multiple courses
]
Distinguish between RNA dependent and DNA dependent Polymerases and identify the process where they are involved.
[
BIOC 3400
]
Given a DNA sequence and restriction enzyme data, analyze a band pattern in a gel and generate a restriction map.
[
BIOC 3400
]
Given an irreversible inhibitor, design an experiment to determine the efficiency of inactivation and the binding affinity.
[
BIOC 4701
]
Integrate amino acid catabolism with other metabolic pathways.
[
BIOC 3300
]
Recall basic principles of regulation of anabolic and catabolic pathways in biochemistry.
[
BIOC 3300
]
Based on the properties of the polynucleotides predict the outcome of differential chemical or enzymatic treatment.
[
BIOC 3400
]
Classify pathways for protein catabolism and their roles in cell biology and metabolism.
[
BIOC 3300
]
Understand autophagy.
[
BIOC 4305
]
Provide evidence for the roles of catalytic RNA in different cellular process such as protein synthesis and RNA splicing
[
BIOC 3400
]
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