Elcetrophoresis

Electrophoresis

1. Table 1: Determining Molecular Weights

Standards Molecular

Weight (d) Distance

Migrated (cm)

94,000 1.3

67,000 1.6

43,000 2.1

30,000 2.9

20,000 3.6

14,000 4.3

Unknown Molecular Weight

Protein 1 1.6 67,000

Protein 2 1.8 58,000

Protein 3 2.1 43,000

Table 1: This table is used in determining the molecular weights of the unknowns proteins that we were given in the experiment. As you can see, when the molecular weights (d) were graphed against the distance migrated (cm) for the standard samples, the molecular weights of the unknowns were determined by comparison. On Chart 1 the points were plotted and a line was drawn so as to determine the unknown protein weights. Protein 1 and protein 3 had distances that directly correlate to distances measured for standards at the 67,000 D and 43,000D, protein 2 when plotted and extrapolated had a molecular weight of approximately 58,000D.

2.

1. In a gel the chemical and physical properties of a protein and disrupt the way it moves through the gel. The movement of the protein in a gel is determined by the charge of the molecules. In an electric field the molecules have to posses a net charge to be able to move. Faster migration or movement is dependant upon having a greater charge over molecules of the same size and shape. The size of the molecules as well as there density, charge and shape can all influence the rate at which they will move through the electric field. SDS-PAGE is not able to fully interact with glycosylated proteins or interact with carbohydrates or nucleic acids at all.

If the disulfide bonds in beta-amylose are not broken properly the molecule could seem larger then it actually is and my not be able to affectively migrate at the correct pace. Also since glutamate has more subunits when they are broken down into linear ones they appear the same as amylase in the migration on the gel.

3. SDS-PAGE is unable to differentiate a multimeric protein; IgG is made up...