365 S2011 L8 - Midterm 1 high 100 low 26 mean 70 1 Protein...

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1 Midterm 1 high 100 low 26 mean 70
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6 Which fractions contains the protein of interest? Was this a good technique to do? Protein purification, trial and error
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7 Bookkeeping 1. Specific activity = total activity/amount of protein 2. Yield = activity after/activity before 3. Fold purification = specific activity after/specific activity before
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8 Yield Specific activity Fold purification Evaluation of a step in the purification
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9 Separation techniques
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10 Salting out Protein solubility is mediated by polar groups on its surface Ions compete with proteins for solvent molecules • (NH4) 2 SO 4 precipitation
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11 Salting out (NH4) 2 SO 4
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12 Chromatography Discovered in 1903 to separate pigments present in plants
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13 Column chromatography 1 Ion-exchange — charge 2 Hydrophobic interaction — hydrophobicity 3 Gel-filtration — size 4 Affinity — specific interaction
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14 Ion-exchange Charged molecules bind to opposite charged groups on the column – Anion exchange (DEAE) – Cation exchange (CM) Affinity depends on the presence of salt and the pH
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