BCH 2333 Lecture Notes - Lecture 10: Proline, Affinity Chromatography, Ion Exchange
14 Feb 2017
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Document Summary
The primary tool in biochemistry to analyze proteins. Not a preparative method can not purify proteins, just analyze. Electric field exerts force on charged molecule. Friction of molecule with solvent and matrix retards movement. Gel usually made from polyacrylamide (polyacrylamide gel electrophoresis = page) Level of crosslinking determines how fast proteins move more crosslinking = more friction. Gel box contains buffy ph 9 peptides have negative charge. Negative and positive poles are connected together to create the magnetic field. Dna gels horizontal, agarose gels, ph 8 buffer. Sds reagent unfolds proteins sodium dodecyl sulfate. Ensures that protein behave the same way in a gel, no matter how they fold. Proteins folded in different shapes would move at different speeds eliminates this factor. Solvates the hydrophobic residues, destabilizes the core of the protein fold. Converts disulfide bonds to free thiols (reductant) Page can be done without sds native gel electrophoresis.
