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Proteins & Proteomics

Course Code: BIOL 3422
Faculty: Science & Technology
Department: Biology
Credits: 3.0
Semester: 15
Learning Format: Lecture, Tutorial
Typically Offered: TBD. Contact Department Chair for more info.
course overview

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

Methods of Instruction

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

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

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

course prerequisites

BIOL 2321 and BIOL 2421



curriculum guidelines

Course Guidelines for previous years are viewable by selecting the version desired. If you took this course and do not see a listing for the starting semester/year of the course, consider the previous version as the applicable version.

course schedule and availability
course transferability

Below shows how this course and its credits transfer within the BC transfer system. 

A course is considered university-transferable (UT) if it transfers to at least one of the five research universities in British Columbia: University of British Columbia; University of British Columbia-Okanagan; Simon Fraser University; University of Victoria; and the University of Northern British Columbia.

For more information on transfer visit the BC Transfer Guide and BCCAT websites.


If your course prerequisites indicate that you need an assessment, please see our Assessment page for more information.