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B. Sc. Biochemistry & Molecular Biology
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Selected tags:
#protein
Account for why a given ligand may be bound tightly by an enzyme or covalently modify an enzyme (transition state analogues).
[
BIOC 4701
]
Analyze optical spectra (absorption, emission, fluorescence anisotropy, LD, CD, IR, Raman) with respect to polypeptide structure and environment and with relation to quantum mechanical basis of a given spectroscopic technique.
[
BIOC 4702
]
Apply Henderson-Hasselbalch equation to calculate the properties of a buffer and the net charge of amino acids and proteins.
[
BIOC 2300
]
Assimilate and integrate the knowledge in a developing field of protein science to deliver a presentation or formulate a literate essay.
[
BIOC 4700
]
Calculate association constants, given tables or graphs of raw data from experiments.
[
BIOC 4700
]
Choose and explain a suitable method to analyze the binding interaction of proteins with small molecules or between proteins.
[
BIOC 4700
]
Describe the basic principles of intracellular signal transduction and discuss how these processes may alter gene expression, protein function and cellular fate.
[
multiple courses
]
Develop a knowledge of the subtleties of amino acid function within the whole protein context. (Post-translation modifications of side chains).
[
BIOC 4700
]
Develop an appreciation of particular techniques in protein science that are unavailable to students in the context of Dalhousie undergraduate program.
[
BIOC 4700
]
Discriminate between and calculate the roles of entropy, enthalpy, and molecular interactions in protein stability, folding and ligand binding.
[
BIOC 3700
]
Discuss the necessity of protein turnover within cells and organisms and the degradative and regulatory mechanisms that govern protein turnover.
[
BIOC 4700
]
Distinguish between cis and trans regulation.
[
BIOC 4404
]
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 protein tagging techniques can be used to determine protein localization or protein interactions in living cells or to affinity-purify proteins from cells.
[
BIOC 4501
]
Explain why the quality of a simulation is more dependent on the speed of a calculation rather than its accuracy.
[
BIOC 4010
]
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
]
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
]
Recognize how changes in lipoprotein metabolism influence atherosclerosis.
[
BIOC 3300
]
Use vector diagrams to explain the major NMR experiments employed for protein NMR.
[
BIOC 4702
]
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
]
Explain cellular pathways for protein transport and modification and their effects on protein function.
[
BIOC 3300
]
Identify the different types of protein factors regulating bacterial gene expression.
[
BIOC 4404
]
Outline in some molecular detail the processes by which genetic information is replicated and expressed, leading to protein synthesis, targeting and turnover.
[
BIOC 1040
]
Compare and contrast the essential features in the digestion and absorption of carbohydrate, lipid and protein.
[
BIOC 4306
]
Describe and interrelate the hierarchical levels of protein structure (1˚ to 4˚) and provide examples of how this structure relates to the function (or dysfunction) of various classes of proteins.
[
multiple courses
]
Draw the structure of a peptide with defined stereochemistry at a given pH.
[
BIOC 3700
]
Explain how dietary carbohydrates, fats and proteins are converted to energy.
[
BIOC 3300
]
Explain the steps of protein synthesis identifying the differences between prokaryotes and eukaryotes.
[
BIOC 3400
]
Understand the established principles of protein folding.
[
BIOC 4700
]
Analyze implications of molecular spectroscopy (absorption, emission, CD, NMR) results on polypeptide structure and environment in direct context of the physical basis of the technique in question.
[
BIOC 3700
]
Design a protein engineering experiment to answer questions about structure/function relationships in new protein.
[
BIOC 4700
]
Explain the biophysics of the non-covalent forces and kinetics and mechanisms governing protein folding and stability.
[
BIOC 4700
]
Explain why ab initio protein folding, or the prediction of tertiary structure from a sequence, is considered one of the most challenging problems in computational biology.
[
BIOC 4010
]
Predict the fate of a protein based on features of the primary sequence.
[
BIOC 3400
]
Apply peptide bond properties and hydrogen-bonding to predict primary and secondary structuring preferences.
[
BIOC 3700
]
Assign two-dimensional homonuclear and heteronuclear NMR data for a polypeptide and apply these assignments for structure determination.
[
BIOC 4702
]
Explain how lipids form membranes and lipoproteins and influence their function, and list different transport mechanisms across membranes.
[
BIOC 2300
]
Explain the problems related to the parametrization of Force Fields.
[
BIOC 4010
]
Recognize nitrogen fixation by plants and bacteria as a starting point for the amino group in proteins.
[
BIOC 3300
]
Analyze data obtained from molecular biology procedures and explain problems associated with expression of human protein products in bacteria or other host cell systems.
[
BIOC 4501
]
Apply the principles underlying structure and folding of simple soluble proteins to the more complex physical environment in which membrane proteins operate.
[
BIOC 4700
]
Classify pathways for protein catabolism and their roles in cell biology and metabolism.
[
BIOC 3300
]
Discriminate the classes of lipoproteins by physical and chemical properties and their functions.
[
BIOC 3300
]
Distinguish Force Field and statistical mechanics energies.
[
BIOC 4010
]
Identify/recognize and explain the roles of the major proteins involved in the process of DNA replication/RNA synthesis and its regulation.
[
BIOC 3400
]
Identify the different types of protein factors regulating eukaryotic gene expression.
[
BIOC 4404
]
Identify the RNA molecules that participate protein synthesis and explain their contributions.
[
BIOC 3400
]
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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