BIO SCI M125 Chapter 21-22: Chapter Summary 10
16 Jan 2017
School
Department
Course
Professor
Document Summary
No ionization of amino acid - titration curve looks like glycine"s. Exothermic = breaking of peptide bond using hydrolysis--> slow because high ea. In order to determine properties/functions of proteins, proteins must be separated. Fractionation - separate proteins based on difference in solutibiliy, ph, temperature, etc. Salting out- at certain levels of salt concentration, the solutbility of proteins is lowered. Some may precipitate out while others remain in solution. Column chromatography - proteins with variation in property move at different rates. Cation -exchange chormoatrphy - positvly charged proteins move though matrix faster. Chromatography - bigger elutes first by taking shortcut. Affinity chromatography- proteins have diffeernt affiinites fro abinding. Slating used before chromography because big sample size makes it need a lot of elute to separate if start w/ chromoagraphy. Applie electric field and migrate unitl reaches pi=ph. Proteins with + charge will go slower because interaction with stationary phase (solid matrix)
