ch05 - Chapter 5: Proteins: Primary Structure Matching A)...

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Chapter 5: Proteins: Primary Structure Matching A) electrophoresis B) hydrophobic C) enzyme-linked immunosorbent assay D) three-dimensional shape E) N-terminal amino acid F) negative charge G) nucleases H) chromophore I) foaming J) high level expression K) 2-mercaptoethanol L) positive charge M) cation exchange 1. One of the reasons primary structure is important for a protein is that this determines the ______ the molecule adopts in aqueous solution. Ans: D Level of Difficulty: Easy Section: 5.1 Learning objective: Polypeptide Diversity 2. If the gene for a protein has been cloned, it may be possible to obtain large quantities of the protein by _________________ in bacteria. Ans: J Level of Difficulty: Moderate Section: 5.2.A Learning objective: Protein Purification and Analysis 3. To help prevent denaturation of proteins in solution, take steps to avoid _________ and adsorption to surfaces. Ans: I Level of Difficulty: Moderate Section: 5.2.A
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Learning objective: Protein Purification and Analysis 4. Molecules that contain a(n)______ are capable of absorbing light. Ans: H Level of Difficulty: Easy Section: 5.2.A Learning objective: Protein Purification and Analysis 5. If antibodies to the protein being assayed are available, a(n) can be developed. Ans: C Level of Difficulty: Moderate Section: 5.2.A Learning objective: Protein Purification and Analysis 6. ______ chromatography is a method of fractionating a protein mixture according to the different polarities of the proteins. Ans: B Level of Difficulty: Moderate Section: 5.2.C Learning objective: Protein Purification and Analysis 7. In order for DEAE to act as an anion exchanger, it must have a ______. Ans: L Level of Difficulty: Moderate Section: 5.2.C Learning objective: Protein Purification and Analysis 8. In ______ chromatography, a protein mixture must be applied to the column at a low pH so that the proteins will have a net positive charge and bind to the column. Ans: M Level of Difficulty: Moderate Section: 5.2.C Learning objective: Protein Purification and Analysis 9. In SDS-PAGE electrophoresis, disulfide-linked protein subunits are separated by first reacting
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them with ______. Ans: K Level of Difficulty: Easy Section: 5.2.D Learning objective: Protein Purification and Analysis 10. Either dansyl chloride or Edman's reagent can be used to identify the ______ of a protein. Ans: E Level of Difficulty: Moderate Section: 5.3.C Learning objective: Protein Sequencing Multiple Choice 11. A fast and common method for determining the concentration of protein in aqueous solution is: A) tandem mass spectrometry. B) salting in with ammonium sulfate. C) drying a portion and weighing the solid. D) measuring light absorption at 280 nm. E)
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This note was uploaded on 11/24/2011 for the course BIO 400 taught by Professor Raganbower during the Winter '10 term at Drexel.

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ch05 - Chapter 5: Proteins: Primary Structure Matching A)...

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