ANSWER:
Both the enzyme kinetics and ligand receptor binding can be analysed with the same equations because of the following reasons:
1. Both enzyme and ligand trigger a series of reaction to occur.
2. Both enzyme and ligand remain unused or unaltered during the reaction.
3. Both enzyme and ligand should have specific structure ( a three dimensional structure) for them to bind to the active site or for them to perform their specific function.
4.Both enzyme and ligands share similar kinetic behaviour and specificity.
5. Both are sensitive to temperature , pH and substrate concentration.
5. Enzyme kinetics and ligand-receptor binding can be analyzed with the same equations. Explain why
D5. Receptor-ligand interactions and enzyme-substrate interactions are similar because they both involve highly specific binding both the ligand and the substrate undergo a chemical change both the receptor and the enzyme alter their activities after the interaction they both rely on covalent binding D 6. Electron carriers like NADH and FADH2 are what type of molecules? enzymes receptors lipids proteins coenzymes
please make sure to draw not just explain Ligand binding to certain receptor tyrosine kinases results in the activation of a sphingomyelinase enzyme. Draw the reaction that shows the sphingomyelinase catalyzed hydrolysis of sphingomyelin to ceramide.
Acetylcholine is the substrate for the enzyme acetylcholinesterase. 1. Suggest what sort of binding interactions could be involved in holding acetylcholine to the active site. 2. The ester bond of acetylcholine is hydrolysed by acetylcholinesterase. Suggest a mechanism by which the enzyme catalyses this reaction. 3. Suggest how binding interactions might make acetylcholine more susceptible to hydrolysis. 4. Structure I is an agonist which binds to the cholinergic receptor and mimics the action of the natural ligand acetylcholine. Structure II,...
Usually a protein-binding curve is a hyperbolic function, with theta on the y-axis and [total ligand] on the x-axis. We can only assume that [Free L]=[L total] when the ligand is in excess of the protein. For example the [protein] would be 0.001 nM and you start adding ligand in .05nm increments. But what would the binding curve above look like if the [receptor]=1 nM: the ligand concentration is no longer in excess of the protein concentration? Would you still...
8. Can same enzyme have different kinetics for different substrates? What is the biological significance that?
You are studying a ligand-gated ion channel. The ligand is a neurotransmitter. Upon binding the neurotransmitter, the ion channel opens and Na+ flows into the cell. The receptor is found on the dendrites of frog neurons. You are going to use one of the patch-clamp variations to study the effect of (1) the neurotransmitter and (2) second (and separately) the effect of an antagonist. Explain the patch-clamp technique variation you would use and why. Explain how you will study the...
Activity 4. Receptor signaling pathway A model of a G protein receptor signaling pathway is represented below. Activation of the signaling pathway results in a cell secreting a neurotransmitter through exocytosis. Activated - Activated adenylyl receptor cyclase GTP АТР CAMP Active G protein Protein- kinase A Inactive Active Protein targets Phosphate group A. Different steps in a signaling pathway can amplify the initial signal of one ligand binding to one receptor. Choose one step in the pathway below that results...
Question 6 The following three molecules are camptothecin analogues that target the topoisomerase I enzyme and are used to treat cancer. LOH Oy “ HO a. Using common structural features generate a simple ligand-based pharmacophore to explain why these compounds may be binding to the same enzyme. List how can pharmacophores be used in a research setting to aid drug discovery? b. ehte c. Given that the compound 3 is metabolised by an esterase in vivo (compounds 1 and 2...
can someone please help with this? 5. Below are two types of enzyme kinetics curves - make careful note of how the axes are different. For each condition below, give the letter(s) indicating the appropriate region(s) of the graph(s). a. Region(s) where the enzyme is saturated with substrate v, (mM/s) b. Region(s) showing equilibration 5 15 20 10 [S] (M) c. Region(s) where an initial velocity is able to be determined d. Region(s) where AG is zero [Product] (MM) 5...
In female mice, both the glucocorticoid (cortisol) receptor and the estrogen receptor are expressed in liver cells (hepatocytes). The control element to which the glucocorticoid receptor binds is a short-strip of DNA that can accommodate the binding of the glucocorticoid receptor dimer. This control element is called a glucocorticoid response element (GRE). It is located1000 bp downstream from the poly-A site for the PEPCK gene. When this gene is activated by cortisol, it helps the hepatocyte to release glucose into...