CellBio_Lecture1_ProteinAnalysis.docx

CellBio_Lecture1_ProteinAnalysis.docx - Protein Analysis...

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Protein Analysis Depending on which properties you want to explore will determine which method you use to study a protein(s) SDS-PAGE: sodium dodecyl sulfate (a detergent, amphiphilic) and poly-acrylamide gel electrophoresis Ions are hydrophilic (head) (polar) Na+ -SO3(CH2)11CH3 (hydrophobic) (tail) (non-polar) This separates proteins by denaturing them then subjecting them to the detergent (SDS - negatively charged) and then running them through the acrylamide gel using an electrode. The charge is added by the SDS, it is needed for the force of the field to cause particles to move, but becomes less important in the gel which sorts primarily by size. Larger molecules move slower in the gel - smaller move quicker. Example in slide 2 shows the purification steps selecting for the protein that is 40,000 peptides in length (40K Da) Detergents work because they are amphiphilic in an asymmetric way. Beta-mercaptoethanol is a reducing agent used to break disulfide bonds HS-CH2-CH2-OH Hydrophobic regions cluster together in water to minimize disruption of H-bonding. Minimize repulsion
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