Insulin binding to an insulin receptor of a cell stimulates tyrosine kinase activity. However, an uncontrollably...

 

Transcribed Image Text:

Insulin binding to an insulin receptor of a cell stimulates tyrosine kinase activity. However, an uncontrollably high number of insulin-insulin receptor binding causes negative impacts on cellular viability. A researcher developed a new ligand X that can act as a scavenger of insulin by binding to an insulin receptor. Researchers find that if given enough time, 85% of insulin receptors form a complex with the ligand X. Consider that the initial concentration of the ligand X is 220mM and the dissociation constant is known to be 5.37 × 10-4 s-1, estimate how long it takes for half of the insulin receptors to form complexes with the ligand X Assume there is no insulin-insulin receptor complex and there is no insulin in the solution. Insulin binding to an insulin receptor of a cell stimulates tyrosine kinase activity. However, an uncontrollably high number of insulin-insulin receptor binding causes negative impacts on cellular viability. A researcher developed a new ligand X that can act as a scavenger of insulin by binding to an insulin receptor. Researchers find that if given enough time, 85% of insulin receptors form a complex with the ligand X. Consider that the initial concentration of the ligand X is 220mM and the dissociation constant is known to be 5.37 × 10-4 s-1, estimate how long it takes for half of the insulin receptors to form complexes with the ligand X Assume there is no insulin-insulin receptor complex and there is no insulin in the solution.

Answer rating: 100% (QA)

To estimate the time it takes for half of the insulin receptors to form complexes with the ligand X ... View the full answer