Regarding macromolecular interactions: A. Diagram the proces…

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Questions

Regаrding mаcrоmоleculаr interactiоns: A. Diagram the process of molecular recognition and association between macromolecules. Describe this in terms of the requirements for macromolecules, like proteins, to interact and form strong, specific interactions. (3 pts.) B. Diagram the four types of non covalent interactions or bonds involved in intermolecular interactions. (3 pts.) C. In your diagrams indicate their relative strengths (exact values are not necessary) (3 pts.) and D. how their strengths are affected by water. (3 pts.) E. In kinase inhibitor assays like we talked about in lecture 3 the KD of the kinase for the inhibitor can be determined by measuring the effect of increasing concentrations of the inhibitor on kinase activity. The results of such assays run with three different anti-cancer drugs are show in the graph to the right. What is the approximate KD for each of the anti-cancer drugs? Which of the three drugs has the highest affinity for the enzyme active site? Propose a mechanism (reason) for the difference in the affinities for the three anti-cancer drugs. (3 pts.)

Regаrding mаcrоmоleculаr interactiоns: A. Diagram the process of molecular recognition and association between macromolecules. Describe this in terms of the requirements for macromolecules, like proteins, to interact and form strong, specific interactions. (3 pts.) B. Diagram the four types of non covalent interactions or bonds involved in intermolecular interactions. (3 pts.) C. In your diagrams indicate their relative strengths (exact values are not necessary) (3 pts.) and D. how their strengths are affected by water. (3 pts.) E. In kinase inhibitor assays like we talked about in lecture 3 the KD of the kinase for the inhibitor can be determined by measuring the effect of increasing concentrations of the inhibitor on kinase activity. The results of such assays run with three different anti-cancer drugs are show in the graph to the right. What is the approximate KD for each of the anti-cancer drugs? Which of the three drugs has the highest affinity for the enzyme active site? Propose a mechanism (reason) for the difference in the affinities for the three anti-cancer drugs. (3 pts.)

Regаrding mаcrоmоleculаr interactiоns: A. Diagram the process of molecular recognition and association between macromolecules. Describe this in terms of the requirements for macromolecules, like proteins, to interact and form strong, specific interactions. (3 pts.) B. Diagram the four types of non covalent interactions or bonds involved in intermolecular interactions. (3 pts.) C. In your diagrams indicate their relative strengths (exact values are not necessary) (3 pts.) and D. how their strengths are affected by water. (3 pts.) E. In kinase inhibitor assays like we talked about in lecture 3 the KD of the kinase for the inhibitor can be determined by measuring the effect of increasing concentrations of the inhibitor on kinase activity. The results of such assays run with three different anti-cancer drugs are show in the graph to the right. What is the approximate KD for each of the anti-cancer drugs? Which of the three drugs has the highest affinity for the enzyme active site? Propose a mechanism (reason) for the difference in the affinities for the three anti-cancer drugs. (3 pts.)

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