CHEM 352 - Introduction to Biochemical Research Techniques
Section: 200
Term: WN 2010
Subject: Chemistry (CHEM)
Department: LSA Chemistry
Requirements & Distribution:
Waitlist Capacity:
With permission of department.
Advisory Prerequisites:
Current or prior enrollment in CHEM 351.
This course counts toward the 60 credits of math/science required for a Bachelor of Science degree.
May not be repeated for credit.
Primary Instructor:

This laboratory course is designed to introduce students to widely used techniques in contemporary biochemistry and analysis of biochemical data. Topics include techniques for the purification and characterization of proteins, enzymes and nucleic acids and some introduction to computational biochemistry and bioinformatics.

The course will comprise 12 lab periods divided into 3 main modules designed to give students broad exposure to widely used techniques in contemporary biochemistry: proteins and enzymes; nucleic acids; and computational biochemistry/bioinformatics. A recitation section, led by a GSI, will replace the traditional l formal lab lecture. This will allow a more thorough discussion of the experiments and the principles underlying them along with their real-world applications. The less formal recitation setting will facilitate question and answer between student and instructor and provide a better understanding of the course material. This in turn, will result in students being better prepared for the next week's experiment. The faculty instructor will, in addition to having overall responsibility for the course, meet with the GSIs on a weekly basis to develop lesson plans and provide detailed guidance on all aspects of the laboratory experiments. The instructor will be available to students on an individual basis through regularly scheduled office hours and informally oversee their lab work through one-on-one interactions during the lab period.

  1. Introduction to buffers, effects of pH and ionic strength on solubility of biological macromolecules Protein and Enzymes
  2. Chromatography: protein separation by ion exchange/or gel filtration; analysis of molecular weights by gel filtration
  3. Protein Purification: a simple (one or two step) purification of a protein overexpressed in E. coli pellet; possibly an enzyme that would be the subject of a later laboratory investigation
  4. Protein Analysis: SDS PAGE of proteins from the previous purification; protein concentration determination using Bradford and ELISA assay for proteins
  5. Enzyme Assay: principles of enzyme assay; steady state kinetics
  6. Enzyme inhibition: determination of mode of action of non-covalent inhibitor or kinetics of irreversible inhibition Nucleic Acids
  7. DNA Purification preparation of plasmid DNA and gel electrophoresis
  8. DNA modifying enzymes, restriction mapping of plasmid
  9. DNA amplification use of PCR to identify particular sequences; DNA fingerprinting
  10. Protein-Nucleic acid interactions, use of gel-shift assay to examine protein nucleic acid interactions e.g., EcoRI & plasmid in Ca; RNaseP protein and RNA; lac repressor and operon Computational Biochemistry
  11. Homology searching, using 'BLAST' to construct a tree, create image of a structure where most conserved regions are highlighted
  12. 3-D modeling exploration of protein-ligand binding interactions through docking and in silico mutagenesis of active site residues

Intended audience: Students at sophomore/junior level who are or intend to be concentrators in Biochemistry and those interested in biochemical techniques. This may include, for example, concentrators in Chemistry, MCDB, and pre-medical students.

Course Requirements: Grades based on written laboratory reports plus in-lab evaluations of students’ skills and comprehension of experiments. A cumulative written in-lab test emphasizing data handling and interpretation will be given at the end of term.

Class Format: 1 hour per week recitation; 4 hour per week lab. Both recitation and lab would be led by the same GSI for continuity.

CHEM 352 - Introduction to Biochemical Research Techniques
Schedule Listing
100 (REC)
Tu 12:00PM - 1:00PM
101 (LAB)
Tu 1:00PM - 5:00PM
200 (REC)
W 12:00PM - 1:00PM
201 (LAB)
W 1:00PM - 5:00PM
400 (REC)
M 12:00PM - 1:00PM
401 (LAB)
M 1:00PM - 5:00PM
NOTE: Data maintained by department in Wolverine Access. If no textbooks are listed below, check with the department.

ISBN: 9780716771081
Lehninger principles of biochemistry, Author: David L. Nelson, Michael M. Cox., Publisher: W.H. Freeman 5th ed. 2008
ISBN: 9780471193500
Biochemistry, Author: Donald Voet, Judith G. Voet., Publisher: John Wiley & Sons 3rd ed. 2004
Syllabi are available to current LSA students. IMPORTANT: These syllabi are provided to give students a general idea about the courses, as offered by LSA departments and programs in prior academic terms. The syllabi do not necessarily reflect the assignments, sequence of course materials, and/or course expectations that the faculty and departments/programs have for these same courses in the current and/or future terms.

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