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?

You have isolated a new protease that cleaves peptide bonds on the carboxyl side of Asp and Glu. Based on the enzyme's inactivation by DIPF, you suspect that it may utilize a mechanism similar to chymotrypsin. The difference in specificity might be explained by the absence of the S1 binding pocket. replacement of serine 195 with a positively charged residue. presence of a positively charged residue in the S1 binding pocket. presence of a negatively charged residue in the S1 binding pocket.

What is meant by intrinsic GTPase activity? Exchange of GDP for GTP on the a-subunit of the G protein Inhibition of GBCR receptor activity Activation of Adenylyl Cyclades Breakdown of cAMP by phosphodiesterase Spontaneous hydrolysis of GTP on the a-subunit of the G-protein

You decide to investigate cell signaling of a pair of newly identified GPCRs, GPCR-W and GPCR-Z. Each binds the same ligand, but activates different downstream heterotrimeric G-proteins that act on adenylyl cyclase. You discover that ligand binding has opposite effects on adenylyl cyclase activity for each receptor. GPCR-W causes an increase in adenylyl cyclase activity, while GPCR-Z causes a decrease in adenylyl cyclase activity. You obtain a cell line expressing GPCR-W, GPCR-Z, the relevant G-proteins, and adenylyl cyclase. There is baseline adenylyl cyclase activity producing a baseline amount of cAMP. You embark on a research project to characterize the following mutations in the components of the signaling pathway. 2. Will each of the following mutations increase or decrease the levels of cAMP inside the cell upon adding the ligand to the cell culture? A mutation in Gi that prevents release of bound GDP. A mutation in Gs that prevents GTP hydrolysis. A mutation in Gi that…