How does a competitive binding assay determine the affinity for an agonist? Specifically, how is the competition measured and the number of receptors/ligands counted?
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How does a competitive binding assay determine the affinity for an agonist? Specifically, how is the competition measured and the number of receptors/ligands counted?
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- What is the importance of understanding the interactions between the receptor binding domain of the spike protein and ACE 2? List four of the interactions (hydrogen bonds) between the spike protein and the receptor (ACE 2)?What is the relative inhibition of the kinase if the substrate concentration equals KS= 50mM and the concentration of the inhibitor equals KI =250mM?My boss has given me the purified extracellular portion of the Notch receptor. As Delta/Notch signaling occurs between cells, I know that both the Notch receptor and and Delta are most likely "comfortable" in the environment of the blood, not the cytosol, nucleus, mitochondria, etc... I want to purify Delta, the signal. What would be true of the most specific purification technique I could choose, i.e. the technique that will result in the fewest proteins in the fraction containing Delta? Do not worry about whether the protein works after fractionation yet. Pick ALL that apply. I would use ion exchange chromatography. I would use size exclusion chromatography I would use affinity chromatography I would use a water based mobile phase of 7.4 I would use an acetonitrile mobile phase with a pH of 7.4 I would use a water based mobile phase of pH 7.2 I would use an acetonitrile phase of 7.2 I…
- Using molecular cloning, a hybrid receptoer is produced that consists of the extracellular domain of the B-adrenergic receptor (B-AR) and the transmembrane and intracellular domains of the EGF receptor (EGFR). Question: What is the stoichiometric ratio of epinephrine to the hybrid receptor (B-AR-EGFR)? 1:1 O 1:4 O 1:2 2:1 O O OWhat are the primary structures of the 1AWJ tyrosine kinase enzyme? What are the secondary structures of the 1AWJ tyrosine kinase enzyme? What is the property of tyrosine kinase enzymes?added ligand concentration of 10 µM is 5 × 10³ s¹. What is the value of the reverse rate constant k_1 = 1 ×10-4 Incorrect Macmillan Learning You have not correctly calculated the value of the reverse rate constant. To begin, calculate the value of k₁ by dividing the rate of receptor-ligand complex formation (the rate of the forward reaction) by the ligand concentration. k₁ = rate forward [L] Then, calculate the value of the reverse rate constant, k_₁, by multiplying the dissociation constant, Kd, and the forward rate constant, k₁. k_1 = Kak₁
- How can you decrease (or stop) the rate of binding for a noncompetitive inhibitor? Could you change the receptor allosteric sites to prevent noncompetitive binding?Sort the following steps of GPCR signal propagation (you may not use all the steps): A) Dephosphorylation of GPCR B) G protein dissociation to adenylate cyclase and GTP binds to the G protein C) Ligand binding to GPCR D) G protein dissociation from GPCR and GDP binds to the G protein E) Synthesis of CAMP F) Activation of PKA G) G protein association to adenylate cyclase H) G protein dissociation from GPCR and GTP binds to the G protein O F, C, H, F, B OC OB, D, A, E, H O C, H, G, E, F OA, G, H, B, EWhat is the relative inhibition of the kinase if the substrate concentration equals Ks And the concentration of the inhibitor equals K, ?
- What is the three-dimensional structure of GPCRs? How does the structure of these receptors determine their functions?Where is this IPT used?you have been asked to develop a drug that could inhibit an enzyme linked receptor. what are the potential pharmacological targets you could design your drug to interact with. which one should you choose and why