BIOLOGY 2B03 Lecture Notes - Lecture 3: Hydrophile, Fluorescent Tag, Bacteriorhodopsin
6 Nov 2017
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Document Summary
Why would a scientist purify proteins: might want to study the folded three-dimensional structure of the protein using x-ray crystallography. Identify the proteins function - what are the substrates and what does the substrate binding do. Protein assay: a method of detecting for the presence of a specific protein and estimating the concentration of the protein, ex. Protein source and extraction: protein should be easily obtained and present in large amounts, ex. In all cases - have to lyse or break open the cell to release all of the proteins inside. Protein stabilization: must be stable at all stages of the extraction process. Stabilizing is the effort to maintain the native structure of the protein and to prevent it from being degraded. Size: gel electrophoresis, gel filtration chromatography, ultracentrifugation, charge. Ion exchange chromatography: gel electrophoresis, polarity, adsorption chromatography, hydrophobic interaction chromatography.
