lecture 5

lecture 5 - Protein Conformation Native conformation-the...

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Protein Conformation Native conformation-the normal tertiary (and quarternary) structure of a protein. Denaturation-the partial or complete disruption or unfolding of the native protein conformation. Treatment with heat, detergent, or strong salts(ions) cause denaturation. Renaturation-restoration of the native conformation. May be accomplished by heating to completely denature and then slowly cooling to allow proper refolding. Cells have proteins called chaperones that assist in protein folding.
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Isolation of Proteins for Analysis Column chromatography is the most common method for separating complex mixtures of proteins. Ion exchange chromatography exploits differences in electrostatic characteristics. Gel filtration chromatography separates proteins based on their sizes. Each separation step results in a partial purification of the protein(s) of interest. Typically, multiple, different separation steps are required to achieve purification, An assay is required to identify the protein of interest.
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To track the purification of a protein and further analyze its biochemical characteristics, some type of biochemical assay is required. Examples: antibody binding, enzymatic assay,
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This note was uploaded on 02/28/2008 for the course BISC 320L taught by Professor Baker,aparicio during the Fall '07 term at USC.

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lecture 5 - Protein Conformation Native conformation-the...

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