BCH210H1 Lecture Notes - Lecture 8: Polyacrylamide, Toothpaste, Protein Structure

• School: UTSG
• Department: Biochemical Engineering and Applied Chemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos, Roman Melnyk, Sian Patterson, Reinhart Reithmeier

Document Summary

Bch210h1(f) lecture 8: sds-page = sodium dodecyl sulfate-polyacrylamide gel electrophoresis, for analyzing protein samples works by separating proteins based on size of polypeptide, sds is a very strong denaturing detergent that dissolves membranes and solubilizes proteins. Sds is actually a very strong ingredient in toothpaste. When protein is put in sds, protein will unfold and lose activity. Sds also locate subunits apart i. e. , with hemoglobin in sds solution, alpha and beta subunits will dissociate, and heme would fall off as well. This molecule disrupts membranes/lipid bilayers because the hydrophobic region is sticking into the inside of lipid bilayer while the sulfate group is on the surface. Sds coats proteins in sds-page and polypeptide chains bind a lot of sds; Sds is present in vast amounts and is negatively-charged, the sds-protein complex, therefore, has an overwhelming negative charge. If you heat up a protein, it will unfold.