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

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