BCH210H1 Lecture 30: L30
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BCH210H1 Full Course Notes
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Analysis of proteins: purification by chromatography, amino acid composition, 20 different amino acids; which ones and how much are present of each, amino acid sequence, the binary structure; going from n-terminal to c-terminal. Protein mixtures: characterization of protein structure and function requires a pure sample, protein samples obtained from cell lysates or by recombinant dna methods are usually mixtures, methods are needed to separate proteins for analysis. Small protein small pores: small proteins are selectively trapped (and slowed) Large protein large pores: large proteins are eluted first, calibrate column with protein of known size, for some proteins we already know their molecular weight, so we are able to calibrate the column based on them. The selected protein will remain bound to the column, when unbound proteins are eluted through the column. Once separated, low molecular weight substrate or ligand is added to the column in excess and competes the bound protein off the column.
