Review_Exam2 - Chapter 5 Given the following two proteins,...

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Chapter 5 • Given the following two proteins, what method would you use to separate a mixture of them? – Protein A 30,000 Da weight, pI 4.8 – Protein B 32,000 Da weight, pI 7.2 a). Gel filtration b). Gas-liquid chromatography c). Ion exchange chromatography d). Affinity chromatography e). Gel electrophoresis
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Chapter 5 • Given the following two proteins, what method would you use to separate a mixture of them? – Protein A 30,000 Da weight, pI 4.8 – Protein B 32,000 Da weight, pI 7.2 a). Gel filtration b). Gas-liquid chromatography c). Ion exchange chromatography d). Affinity chromatography e). Gel electrophoresis
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Chapter 5 • Given the following two proteins, what method would you use to separate a mixture of them? – Protein A 30,000 Da weight, pI 4.8 – Protein B 61,000 Da weight, pI 5.2 a). Gel filtration b). Gas-liquid chromatography c). Ion exchange chromatography d). Affinity chromatography e). Gel electrophoresis
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Chapter 5 • Given the following two proteins, what method would you use to separate a mixture of them? – Protein A 30,000 Da weight, pI 4.8 – Protein B 61,000 Da weight, pI 5.2 a). Gel filtration b). Gas-liquid chromatography c). Ion exchange chromatography d). Affinity chromatography e). Gel electrophoresis
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Chapter 5, #19, Companion • The molecular mass of a protein is 6.8 kD according to SDS-PAGE. Yet, treatment with 2- mercaptoethanol first, then SDS-PAGE yields two bands, 2.3 kD and 4.5 kD. What happened? The protein is composed of two chains connected via a disulfide bond. 2-mercaptoethanol reduces the S-S bond, releasing the peptides. Chain1(2.3 kD)-S-S-Chain2(4.5 kD)
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• What is the primary structure of a protein? • What is the secondary structure of a protein?
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This test prep was uploaded on 04/19/2008 for the course BIOL 3324 taught by Professor Ziburkus during the Spring '07 term at University of Houston.

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Review_Exam2 - Chapter 5 Given the following two proteins,...

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