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Myoglobin structure and function: A multiweek biochemistry laboratory project
Author(s) -
Silverstein Todd P.,
Kirk Sarah R.,
Meyer Scott C.,
Holman Karen L. McFarlane
Publication year - 2015
Publication title -
biochemistry and molecular biology education
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 39
eISSN - 1539-3429
pISSN - 1470-8175
DOI - 10.1002/bmb.20845
Subject(s) - myoglobin , biochemistry , function (biology) , chemistry , computational biology , biology , microbiology and biotechnology
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. © 2015 by The International Union of Biochemistry and Molecular Biology, 43(3):181–188, 2015.