SDS PAGE - A ndrew Castleman SDS PAGE Sodium dodecyl...

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Andrew Castleman SDS PAGE Sodium dodecyl sulfate is a detergent that is able to unravel proteins by disrupting all non-covalent bonds and interactions the protein has with itself. When the amphiphilic SDS interacts with the protein it gives the overall complex a very large negative charge to molecular weight ratio. The charge to mass ratio is constant for all polypeptides. So much SDS interacts with the protein that the charge of the complex is essentially due to how many SDS molecules are in the complex. The negatively charged, denatured protein can then be studied using electrophoresis in a polyacrylamide gel. The proteins will separate by size as the smaller proteins will move more easily and the larger proteins less easily resulting in the smaller proteins traveling farther. This allows us to determine the number of distinct subunits formed when SDS denatures a purified protein and when compared to a standard containing proteins of known molecular weight, provides a way to estimate the molecular weight of the subunits/protein. By taking the log of the molecular weights of the proteins in the standard solution and plotting them against the distance traveled, we can establish a record of how
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This note was uploaded on 04/22/2011 for the course BIOCHEM 412 taught by Professor Thomas during the Spring '11 term at Tennessee Martin.

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SDS PAGE - A ndrew Castleman SDS PAGE Sodium dodecyl...

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