Myoglobin structure and function: A multiweek biochemistry laboratory project.
We have developed a multiweek laboratory project in which students isolate myoglobin and characterize its structure, function, and redox state. The important laboratory techniques covered in this project include size-exclusion chromatography, electrophoresis, spectrophotometric titration, and FTIR spectroscopy. Regarding protein structure, students work with computer modeling and visualization of myoglobin and its homologues, after which they spectroscopically characterize its thermal denaturation. Students also study protein function (ligand binding equilibrium) and are instructed on topics in data analysis (calibration curves, nonlinear vs. linear regression). This upper division biochemistry laboratory project is a challenging and rewarding one that not only exposes students to a wide variety of important biochemical laboratory techniques but also ties those techniques together to work with a single readily available and easily characterized protein, myoglobin.
Department of Chemistry, Willamette University, Salem, Oregon, 97301.
Todd P
TP
Silverstein
Department of Chemistry, Willamette University, Salem, Oregon, 97301.
Sarah R
SR
Kirk
Department of Chemistry, Willamette University, Salem, Oregon, 97301.
Scott C
SC
Meyer
Department of Chemistry, Willamette University, Salem, Oregon, 97301.
Karen L McFarlane
KL
Holman
D001671:Biochemistry / Q000193:education* / Q000379:methods*; D006801:Humans; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D013329:Structure-Activity Relationship
D009211:Myoglobin
active learning; biophysical methods; computational biology; inquiry-based teaching; laboratory exercises; protein structure function and folding