Proteins & Proteomics

Curriculum guideline

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Course
BIOL 3422
Discontinued
No
Course code
BIOL 3422
Descriptive
Proteins & Proteomics
Department
Biology
Faculty
Science & Technology
Credits
3.00
Start date
End term
Not Specified
PLAR
No
Semester length
15
Max class size
35
Contact hours
Lecture 3 hours per week Tutorial 1 hour per week
Method(s) of instruction
Lecture
Tutorial
Learning activities

Instruction will be a combination of lecture, guest lectures, seminar, in-class activities and student presentations.

Course description
This course is focused on the fundamental aspects of proteins, including their chemical and physical structure, synthesis and stability, and function. In addition to these fundamentals, classical and contemporary methods used to purify and analyze proteins, and determine or predict their structure will be covered. Current topics in protein structure and proteomics will also be examined.
Course content

1. Review of amino acid structure

  • Classifications
  • Abbreviations
  • Chemical structure

2. Amino acid biosynthesis

  • Review of nitrogen metabolism
  • Biosynthesis of nonessential amino acids starting from different precursors
  • Synthesis of molecules derived from amino acids

3. Primary structure

  • Sequencing methods
  • Sequencing applications

4. Secondary structure

  • Alpha helix
  • Beta turns
  • Beta sheets

5. Supersecondary structure

  • Motifs
  • Domains

6. Tertiary structure

 

7. Quaternary structure

 

8. Assisted folding

  • Molecular chaperones
  • Chaperonins

9. Methods to determine protein structure

  • NMR spectroscopy
  • X-ray crystallography
  • Mass spectrometry
  • Electron microscopy

10. Proteomics

  • Protein data bank
  • Other protein databases

11. Enzyme kinetics

  • Introduction and classification
  • Active sites
  • Transition states
  • Kinetic parameters
  • Measuring enzyme kinetics
  • Enzyme inhibitors

12. Protein regulation

  • Proteolytic cleavage
  • Phosphorylation
  • Allostery
  • Complex regulation

13. Membrane proteins

  • Role in biosignaling
  • G-protein receptors
  • Receptor tyrosine kinases
Learning outcomes

After completion of this course, students will be able to:

1.  Identify the structures of the common amino acids in proteins

2.  Describe the biosynthesis of the common amino acids in proteins

3.  Describe the common elements found in primary, secondary, tertiary and quaternary structure

4.  Explain the role of molecular chaperones

5.  Explain the different methods used to identify protein structure

6.  Describe the typical Michaelis-Menten kinetics of enzymes, and also describe the effects of enzyme inhibitors

7.  Explain protein regulation, using specific examples

8.  Analyze the structure and function of membrane proteins

Means of assessment

Evaluation will be carried out in accordance with Douglas College policy. The instructor will present a written course outline with specific evaluation criteria at the beginning of the semester. Evaluation will be based on the following:

Evaluation Marks
Quizzes and/or assignments   15-25
Group project  5-15
Midterm examination 20-30
Final examination 30-40
Total   100

 

 

Textbook materials

Students should consult the Douglas College Bookstore for the latest required textbooks and materials. For example textbooks and materials may include:

DL Nelson and MM Cox. Lehninger – Principles of Biochemistry (Current edition).  New York: Worth Publishers

Prerequisites

BIOL 2321 and BIOL 2421

Corequisites

None

Equivalencies

None

Which prerequisite

None