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Practical Methods in Biochemistry
MB&B 340
Fall 2017 not offered
Crosslisting: CHEM 390

This course centers on currently used techniques for protein separation, characterization, and purification, such as ultracentrifugation, gel electrophoresis, and chromatography. These topics will be introduced within the general context of the behavior of macromolecules in solution. The relative stability of proteins in different media, the forces stabilizing protein structure, and the interaction of proteins will be discussed. We will explicitly consider different techniques used to study proteins. Relatively novel techniques to be discussed include surface plasmon resonance, microarray methods and mass spectrometry, and single molecule microscopy. In the course, we will go through three or four different protein purification protocols and discuss the methods used in each one. We will also touch upon the commonly used spectroscopic techniques used to characterize proteins, including absorption, fluorescence, and circular dichroism. The course will focus on biochemical techniques and understanding the physical principles underlying these techniques and will also discuss tactics for optimizing established isolation and purification procedures and for isolating and characterizing an unknown protein.

The course content is appropriate for advanced undergraduates (juniors/seniors) and beginning graduate students from chemistry, biology, molecular biophysics or MB&B.
Credit: 1 Gen Ed Area Dept: NSM MB&B
Course Format: Lecture / DiscussionGrading Mode: Graded
Level: UGRD Prerequisites: [MB&B208] OR [CHEM383 or MB&B383]
Fulfills a Major Requirement for: (MB&B)

Last Updated on MAY-29-2024
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