BCH 2333 Lecture Notes - Lecture 10: Sodium Chloride, Mass Spectrometry, Molar Mass
16 Dec 2017
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Page: native and denaturing - based on charge and mass. Denaturing: proteins are unfolded by sds, adds extra negative charge. Larger proteins move more slowly, won"t make it as far down the gel. Like-charged proteins sticks to the resin, more charged proteins stick harder. Elute proteins with charged mobile phase including lots of ions (ex. Nacl with lots of cl- for negatively charged stationary phase) Ions replace proteins and the protein ows out of the column. Gel ltration chromatography: based on size (molar mass) Small proteins stick into pores of polymer beads. Proteins small enough to stick into pores more slowly. Large proteins don"t t in pores and elute slowly. Uses a stationary (inert) support with af nity tags attached. Tag can only be bound by speci c protein. Only proteins that bing to the tag stick to the stationary phase and unwanted proteins can be washed away.
