Laboratory teaching fundamental techniques in biochemistry. $40 lab fee. Cross-listed as BIOL 420L. Students majoring in Biology or Chemistry must earn a grade of C or higher. Prerequisites: BIOL 110 and CHEM 210.
Prerequisite(s) / Corequisite(s):
BIOL 110 and CHEM 210.
Course Rotation for Day Program:
Most current editions of the following:
Experimental procedures should be taken from texts such as:
Fundamental Laboratory Approaches for Biochemistry and Biotechnology
By Ninfa & Ballou (John Wiley and Sons, Inc.) Recommended
Experiments in Biochemistry: A Hands-On Approach
By S.L. Farrell & L.W. Taylor (Thompson Brooks/Cole) Recommended
Modern Experimental Biochemistry
By Boyer (Benjamin Cummings) Recommended
To perform broadly applicable lab techniques in biochemistry.
To acquire facility with laboratory equipment used in modern experimental biochemistry.
To use the scientific method to design and conduct experiments.
To perform and evaluate experiments in the isolation, purification, and analysis of macromolecules.
To use critical analysis skills to interpret data and draw conclusions.
To learn scientific writing.
Accomplish experimental manipulations using basic lab equipment such as micropipettrs, microcentribuges, ultracentrifuges, spectrophotometers, agarose and polyacrylamide gel electrophoresis chambers.
Write lab reports based on the format used in scientific journals.
Perform calculations to determine molarity, serial dilution, and % weight/volume.
Use the scientific method in the design and analysis of experiments.
Manipulate buffers with different buffering capacity by manipulating buffers with different concentrations, pH values, pKa values.
Perform isoelectric focusing to determine the isoelectric point of different proteins.
Successfully execute methods in protein isolation and analysis such as differential centrifugation, differential solubility, dialysis, column chromatography, and gel electrophoresis to isolate and purify a specific enzyme from living cells.
Compare and contrast the efficiency and uses of different types of column chromatography in separation, detection, and analysis of macromolecules.
Determine the reaction kinetics and inhibition of specific enzymes.
Use spectrophotometry and colorimetric methods to determine concentrations of protein in unknown samples.
Determine kinetic parameters of specific enzymes for specific substrates and inhibitors.
Detect the presence of specific proteins in a mixed sample using Western blot techniques.
Isolate and analyze subcellular organelles.
Investigate factors that control protein-ligand binding interactions.
NOTE: The intention of this master course syllabus is to provide an outline of the contents of this course, as specified by
the faculty of Columbia College, regardless of who teaches the course, when it is taught, or where it is taught. Faculty members teaching this
course for Columbia College are expected to facilitate learning pursuant to the course objectives and cover the subjects listed in the topical
outline. However, instructors are also encouraged to cover additional topics of interest so long as those topics are relevant to the course's
subject. The master syllabus is, therefore, prescriptive in nature but also allows for a diversity of individual approaches to course material.