You are determing the structure of a new protein. When you perform molecular exc

Question

You are determing the structure of a new protein. When you perform molecular exclusion chromatography you determine that the size of the protein is 300 kDa. Next you perform a SDS-PAGE and observe one protein band at 150 kDa. After running the gel you realize that you forgot to add beta-mercaptoethanol BME) to the protein mixture before running the gel, so you repeat the analysis. The second time you run DS-PAGE (this time with beta-mercaptoethanol) there are 2 protein bands- one at 100kDa and one at 50kDa Given what you know about the levels of protein structure, protein purification, and protein detection techniques, answer the following questions about the structure of this proteir a) What is the function of SDS? (May be more than one answer, choose all that are correct) Breaks peptide bonds Disrupts interactions needed for secondary structure Disrupts weak interactions for tertiary and quaternary structure Disrupt disulfide bonds Gives the protein a negative charge b) What is the function of beta-mercaptoethanol? (May be more than one answer, choose all that are corre Breaks peptide bonds Disrupts weak interaction needed for secondary structure Disrupts weak interactions needed for tertiary and quaternary structure Disrupts disulfide bonds Gives the protein a negative charge

Explanation / Answer

a) What is the function of SDS?
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b) What is the function of beta-mercaptoethanol?
Correct options:

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