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Question: Protein folding A mutation that changes an alanine residue in the interior of a protein into val…

Question: Protein folding  A mutation that changes an alanine residue in the interior of a protein into val...

Protein folding A mutation that changes an alanine residue in the interior of a protein into valine is found to lead to a loss of the protein specific activity. However, activity is regained when a second mutation at a different position changes an isoleucine residue into glycine. How might this second mutation lead to a restoration of activity? Draw the pairs of amino acids to illustrate your answer. Protein Purification You have a mixture of three proteins: Protein X, MW 15 kDa, pl 4.5 Protein Y, MW 75 kDa, pl 8.5 Protein Z, MW 25 kDa, pl 5.5 pl refers to the pH value when the net charge of a protein is equal to zero (positive and negative are balanced). Thus, proteins with pl values lower than 7.0 are acidic, i.e. they are negatively charged at neutral pH: whereas proteins with pH above seven are basic, i.e. they are negatively charged at neutral pH. In what order would proteins X, Y, and Z elute from a size exclusion (gel filtration) column? Would you expect all three proteins to resolve completely by size exclusion chromatography? Briefly, why or why not?

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