1. In your new job at the Nutrasweet company, you are investigating which transp
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1. In your new job at the Nutrasweet company, you are investigating which transport proteins are responsible for carrying your newest low calorie sugar substitute (glucostatic) into cells. You have identified a protein that you have named Skinny that you believe is important for transporting glucostatic across the membrane. To investigate whether Skinny is a transporter for glucostatic, you plan to engineer a series of mutations that will change amino acids in the structure of the Skinny protein. a. You believe that the extracellular domain of Skinny binds glucostatic, a negatively charged molecule, during the uptake process. You hypothesize that there are specific amino acids in the extracellular domain that may play a role in binding o glucostatic. Based on your knowledge of amino acid chemical properties that you learned in cell biology, you select one amino acid that could interact with glucostatic. Explain your choice. b. You look at the primary sequence of Skinny and have found the amino acid that you selected in part A and it is located in the extracellular domain. To determin whether this amino acid binds glucostatic, you plan to engineer a mutant prote that will still bind glucostatic. Which amino acid could you substitute in for answer from A that will allow Skinny to still bind glucostatic. Explain your answer c. The next mutant protein you design will eliminate the binding of glucostatic to the extracellular domain of Skinny. Which amino acid could you substitute in for your answer from A that will disrupt glucostatic binding? Explain your answer d. Skinny has a transmembrane domain along with an intracellular and extracellular domain. Name three amino acids that could be found in the transmembrane domain. Explain your answer e. You hypothesize that the structure of the transmembrane domain of Skinn alpha helix. Before y test your hypothesis by engineering a mutant protein that disrupts the alpha helical structure of Skinny. Based on your knowledge of amino acid chemical properties and the stability of alpha helical structures, which amino acid would you engineer into the alpha helix to destabilize the secondary structure of the transmembrane domain of Skinny. Explain your answer ou can receive your promotion and bonus, your boss asks you toExplanation / Answer
1a) Lysine Arginine or Histidine since they are positively charged amino acids and will have high binding affinity to Glucostatic.
b) Either of the three positively charged Amino acids i.e. Lysine, Arginine and Histidine can be substituted by one another that will allow Skinny to bind to Glucostatic because of their positive charge.
c) This time we will take an amino acid that has very low binding affinity to negatively charged molecules like Glutamate or Aspartate which are negatively charged amino acids hence would result in Skinny not binding to Glucostatic.
d) Amino acids that could be found in Transmembrane domain are Alanine, Valine and Glycine which are hydrophobic amino acids because of their alkyl side chains. Transmembrane part is hydrophobic in nature because of lipid bilayer hence hydrophobic interactions will be more stable.
E) To desrabilize the secondary alpha helical structure, Proline amino acid can be integrated into the helix through mutation. Proline is a Hydrophobic amino acids with a bulky side chain that causes steric hinderance, which makes it unviable to be folded into an alpha helix.
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