Answer the following questions:
a) What is special about the E coli BL21(DE3)pLysS cells used for gene expression?
b) In what structural form is the expressed gdhA gene synthesized in the E coli host cells?
c) What physical attributes of SDS-PAGE gels allow the separation and molecular weight determination of polypeptides?
d) Given the size of the gdhA gene of ~1362 bp, what is the theoretical size of the expressed protein?
e) Does your answer from (d) agree with the MW size of your expressed protein, and if not, Why?
Answer the following questions: a) What is special about the E coli BL21(DE3)pLysS cells used for...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...