Chapter 3. 3.1 SDS-PAGE Analysis

Introduction

Assessments for Animated Techniques
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3.1 SDS-PAGE Analysis

Question 3.1

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_feedback_correct: Correct. _feedback_incorrect: Incorrect.

Question 3.2

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_feedback_correct: Correct. _feedback_incorrect: Incorrect.

Question 3.3

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_feedback_correct: Correct. _feedback_incorrect: Incorrect.

Question 3.4

After running gel chromatography on your purified protein sample, you notice that the molecular weight of the protein corresponds to 120 kDa.

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_feedback: The protein is a trimer composed of two 50 kDa subunits and one 20 kDa subunit.

Question

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_feedback: The 20 kDa subunit is really two peptide subunits, a 15 kDa subunit and a 5 kDa subunit, held together by a disulfide bridge.

Question 3.5

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_feedback_correct: Correct. _feedback_incorrect: Incorrect.

Question 3.6

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_feedback_correct: Correct. _feedback_incorrect: Incorrect.

Question 3.7

Treating proteins with SDS and heat allows all of the proteins to have the same Uoxw57QEgrI51Mb7OOpscQ8O0dUTxwmJ9q3qnxMvx1KFwcaIcpLWEL4te/FMVnBe, allowing the proteins to be separated based on their size.

_feedback_correct: Correct. _feedback_incorrect: Incorrect.

Question 3.8

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_feedback: Some of the protein may have a posttranslational modification such as phosphorylation or acetylation that has occurred. This could be tested for by treating the sample with a phosphatase or a deacetylase prior to SDS-PAGE analysis.

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