Chap 3 - Chap 3 Proteins differ by 1. 2. 3. 4. Size- gel...

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Chap 3 Proteins differ by 1. Size - gel filtration, dialysis, SDS PAGE 2. Shape - plain electrophoresis 3. Affinity - affinity chromatography 4. Charge –iso- electric focusing, plain electrophoresis, ion exchange chromatography Plain electrophoresis - charge/size/shape 2D gel chromatography - charge/size Gel Filtration - method of protein or DNA purification, where differences in size are used to separate the components of a complex mixture. Produces good seperations, used to estimate molecular weight if proteins are globular. Big proteins leave first, only small molecules can enter beads which are made of dextran or sephadex a bacteria starch Dialysis - protein separated from small molecules thru semi permeable membrane, big molecules are in the bag and the small molecules are outside the bag. Ion-Exchange -proteins separated by net charge, positive proteins bound to negatively charged beads, and negatively charged proteins flow through. Affinity Chromatography - purifying proteins by taking advantage of proteins affinity for specific chemical groups. This is most effective when interactions of protein and molecule that is used as bait is highly specific. Plain Electrophoresis - The use of an electric current to separate large molecules (such as proteins) from other molecules for analysis. Molecule with net charge will move through magnetic field, power for separating proteins like DNA and RNA. (Molecules move toward opposite charge) Gel Electrophoresis - A type of electrophoresis in which the molecules in a sample moves through a gel composed of agarose or polyacrylamide. Iso Electric Focusing
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This note was uploaded on 10/28/2008 for the course BIO CHEM 101 taught by Professor Dunno during the Spring '08 term at Rutgers.

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Chap 3 - Chap 3 Proteins differ by 1. 2. 3. 4. Size- gel...

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