BCH210H1 Lecture Notes - Lecture 11: Elution, Protein Structure, Blackboard

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Sian Patterson

Document Summary

Ch 2 (q 1(abc), 2(abc), 3, 4, 19b) Midterm room assignments have been posted on blackboard. Lecture 11/12 - intro to proteins and protein structure. Characterization of protein structure and function requires a pure sample. Protein samples obtained from cell lysates or by recombinant dna methods are usually mixture. Methods are needed to purify proteins for analysis. Column separates by size or molecular weight --> you can buy them commercially now. Column matrix (resin) consists of porous beads with varying pore size. Calibrate with protein of known size (can run albumin, for example) Smaller proteins are selectively trapped --> take longest bc they run through entire bead. Larger proteins elute first and get through bc they aren"t trapped. Absorbance is used to identify the proteins --> below is an elution profile. The kinks at the very end are the salts. Can use an antibody to identify your protein. Most selective because you are using a property unique to it.