Separation of Proteins by Gel Electrophoresis

Flashcards covering key concepts from the lecture on protein separation by gel electrophoresis.

What factors enable proteins to perform various biological functions?

Proteins differ in their charge, shape, size, and solubility.

What is the isoelectric point of a protein?

The pH at which the protein has equal negative and positive charges, resulting in a net charge of zero.

What types of amino acids contribute to a protein's negative charge at physiological pH?

Glutamic acid and aspartic acid.

Which amino acids are responsible for a protein's positive charge at physiological pH?

Lysine, arginine, and to a lesser extent, histidine.

How does the charge of amino acids change with pH?

At high pH, glutamic and aspartic acids become negatively charged, while lysine and arginine become uncharged.

What are the general shapes of proteins?

Spherical, elliptical, or rod-like.

What describes proteins that are in their normal, biologically active forms?

Native proteins.

What factors affect a protein's electrophoretic migration rates?

Magnitude of charge, size, and shape of the native protein.

What is electrophoresis?

A technique used to separate, identify, or purify macromolecules based on size, charge, and conformation.

What is Agarose and its role in gel electrophoresis?

A polysaccharide used to make gels for electrophoresis, allowing for the separation of charged molecules.

Which protein is the most abundant in serum and has a fast electrophoretic migration rate?

Albumin.

What happens during gel staining for visualization in electrophoresis?

Proteins are stained to visualize their presence on the gel after undergoing electrophoresis.