what are the steps in protein breakdown using gel electrophoresis?

Answer 1

proteins are not broken down in gel electrophoresis.

they are seperated by size (smaller ones travel farther down the gel), but they are not denatured or broken down by the electrophoresis

Answer 2

Protein breakdown? I wasn't aware that a gel broke anything down... separate pieces based on molecular size, yes, but I always thought enzymatic action was responsible for cutting them into discrete bits to begin with.

Here's how I understand gel electrophoresis: Treating a genetic sample with a specific enzyme that cuts the DNA at a desired sequence of peptides gives you bits that you know begin and end with a certain sequence. Pipetting samples of this into the wells of an electrophoresis gel along with a molecular dye and running a current through it causes the charged fragments to move through the gel matrix in the direction of current flow (and you have to be careful you have the polarity right, or they'll just run out the well end of the gel) The lower the current, the slower it'll go, but the better separation you'll get. After a certain time (dependant on current and the size of the gell you're using), you stop the current and the dyed fragments will form discrete bands where they finally stopped, giving you dark bands that tell you, generally, how big each fragment is.

Answer 3

Proteins are not broken-down during electrophoresis. They just get separated based on their size and charge. In case of SDS-PAGE (Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis), SDS is used to mask the intrinsic charge of the protein so that they all have the same charge. Thus, the proteins get separated based just on their molecular weight.
Proteins have to be broken down into their subunits before electrophoresis by breaking the disulphide bonds using b-mercaptoethanol.

Answer 4

Gel Electrophoresis is not used for protein, or as far as I know. It's used in DNA printing. It has a electrical charge that separates the smaller strands of DNA from the larger ones.

Answer 5

it's basically unfolding of the native state & the breaking of hydrogen bonds & disulphide bonds to make the protein a long chain of amino acid residues......