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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