how ligand binding and conformational changes results
in G-protein activation
Heterotrimeric G proteins, are activated by G protein-coupled receptors.They are bound to the inner surface of the cell membrane.and consist of the Gα and the tightly associated Gβγ subunits [beta (β), and gamma (γ) subunits].In normal state Gα is bound by GTP. When a ligand binding activates the G protein-coupled receptor, it induces a conformational change in the receptor that allows the receptor to function as a guanine nucleotide exchange factor (GEF) that exchanges GDP for GTP turning the GPCR "on". This exchange activates G protein and triggers the dissociation of the Gα subunit (which is bound to GTP) from the Gβγ dimer and the receptor as a whole.
how ligand binding and conformational changes results in G-protein activation
Positive cooperativity is when binding of a ligand to a protein results in a conformational change that allows increased binding affinity at other ligand binding sites in the same molecule. Select one: True False
Ligand binding to a G-protein coupled receptor (GPCR) results in activation of a single G- protein and then the receptor deactivates. O True False When an activated receptor relays the signal along more than one pathways this is called convergence. O True OFalse Which of the following best describes digestive enzymes? O Hydrolases OLigases Kinases Transferases Decarboxylases Most digestive enzymes are released from cells in an inactive form. True False denatures Protein digestion in humans (and other mammals) begins in...
Epinephrine is a ligand for the beta-adrenergic receptor. When activated the beta-adrenergic receptor undergoes a conformational change that results in the activation of the G protein GsLaTeX: \alpha α . Which of the following secondary messengers would you expect to be increased when epinephrine binds to a beta-adrenergic receptor? DAG cGMP cAMP Ca2+ phospholipase C IP3
The binding of a ligand to a receptor is important for allowing external signals to affect intracellular processes. Which property of receptor proteins is key for this signaling to occur? Select one: a. Non-reversible binding to ligand b. Non-rigid structure that allows for conformational changes when a ligand binds c. Non-specific interactions with extracellular molecules d. Non-specific interactions with intracellular molecules
A binding protein binds to a ligand with Kd=30nm. What is the
concentration of ligand when the [L] when the fraction
bound,,
is a) 0.25, b) 0.6 and c) 0.95.
similarities and differences between the lock-and-key, induced fit, and conformational selection models of protein-ligand interactions
If 20% of binding sites of a protein are occupied by its ligand when the concentration of the ligand is 1mM, what is the Kd of this protein-ligand interaction? A. 0.2mM B. 1mM C. 2.5 mM D. 4mM E. 5mM
You are characterizing the binding of a ligand to a protein. Knowing that the rate of association between the protein and ligand is diffusion controlled and that the KD is expected to be around 100 µM, a) What do you expect that half-life of the complex to be? b) What method would you choose to measure the KD? Briefly describe why the method is appropriate
Short answer questions: 21. Protein A has a binding site for ligand L with a Ka of 10-6 M. Protein B has a binding site for ligand L with a Ka of 10'M. (a). Which protein has a higher affinity for ligand L? Explain your reasoning. (b). At what concentration of ligand L is proteins A half-saturated. At what concentration of L is protein B half-saturated. [L] y = [L] + Ka 22. A protein binds to a ligand L...
A binding protein binds to a ligand L with a K_d of 400 nM. What is the concentration of ligand when is a) 0.25, b) 0.6, c) 0.95?