a molecule that lowers cholesterol levels in humans interacts with the enzyme HMA-COG reductase. how do you describe their interaction biochemically? what experiment would you do?
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a molecule that lowers cholesterol levels in humans interacts with the enzyme HMA-COG reductase. how do you describe their interaction biochemically? what experiment would you do?
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- Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)Cone snails are carnivores that inject a powerful set of toxins into their prey, leading to rapid paralysis. Many of these toxins are found to bind to specific ion-channel proteins. Why are such molecules so toxic? How might such toxins be useful for biochemical studies?In a biochemical pathway where A--1--B--2--C--3--D. If D is a competitive inhibitor of enzyme 1, what happens?
- Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed.What is the relationships between Kcat and that of stability. How is Kcat related to activation energy?
- Give an example of a noncompetitive inhibitor and its target enzyme. Draw a hypothetical Michaelis-Menten curves in the presence and absence of the noncompetitive inhibitor. Discuss the effects of noncompetitive inhibition and the reasons for these effects on the values of Km and Vmax.In proteins involved in blood clotting to heal a wound, the amino acid GLU is often chemically modified to carboxy-glutamic acid (abbreviated GLA, shown in diagram at pH 7) by a carboxylase enzyme in the blood. The pKa values for the two ionizable protons in the R-group of GLA are shown. A sample of the octopeptide ILE-GLA-ARG-GLY-MET-ARG-PHE-SER was digested with trypsin, adjusted to pH 13, and applied to an anion exchange column. The peptides were then eluted from the column using a pH gradient from 13 to 0.5. Write the order of the products (no structures required) at the pH they would elute from the column and indicate the pH value. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.6 and 2.2 respectively. (Relevant pKa values are 2.2, 3.2, 4.8, 9.6, and 12.5).Hexokinase is an important enzyme in the metabolism of glucose. If theconcentration of hexokinase in our eukaryotic cell is 20 μM, how many glucose molecules are present per hexokinase molecule?
- The enzyme mutase which is important for the synthetic of tyrosine and phenylalanine in saccharomyces cerevisiae has been studied as an example of an allosteric enzyme. Tyrosine acts as a negative effector for this enzyme. What effects would you see on the action of the enzyme were you to increase the concentration of tyrosine? The chorismate mutase would shift to its R conformation The curve showing the kinetics or chorismate mutase would shift to the right The curve showing the kinetics of chorismate mutase would shift to the left The chorismate mutase would become saturated more rapidlya. Estimate KM and Vmax for the uninhibited reaction from the first graph. Whatdifficulties do you find in getting accurate values?b. Make a Lineweaver-Burk (double reciprocal) plot to determine KM and Vmax again.What advantages do you see with the second method? c. Use the Lineweaver-Burk method and the table of data for the inhibitors to determine the kind of inhibition for each inhibitor.How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?