• What happens to the functionality of a denatured enzyme? • How can that result be explained with the help of the lock and key model?
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- Q) Can a reversible enzyme be regulated by product inhibition? Justify your reasoning. (4 sentences MAX)Q: Select the features of the structure and functioning of allosteric enzymes: a) are metabolic pathway limiting enzymes b) when interacting with ligands do not show a cooperative effect c) are monomeric proteins d) have spatially separated active and regulatory centers e) do not exhibit regulatory properties during dissociation of the molecule into protomers15 All of the following are characteristics of all enzymes EXCEPT? Select the correct response: • They are made up entirely of amino acid residues. They are water-soluble proteins with spherical shape. They have amino acid side chains that are critical for facilitating catalysis. They facilitate catalysis without being consumed in the over-all process. They have a catalytic region that stabilizes the substrate's transition state.
- Which of the following analogies best describes the induced-fit model of enzyme-substrate binding? a hug between two people a key fitting into a lock a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy the fitting together of two jigsaw puzzle pieces1. Describe the two ways by which the activity of an enzyme can be inhibited.Q: establish a correspondence between letter and number (NOT A GRADED QUESTION) A. Stimulates the secretion of the enzyme into the blood. B. Accompanied by a change in the number of protomers in the protein. C. Changes the primary structure of the protein. D. Reduces the charge and changes the conformation of the enzyme. E. Reduces the amount of enzyme in the cell. 1. Partial proteolysis 2. Association - dissociation 3. Dephosphorylation.
- 1. Construct a model that demonstrates how enzyme catalyzed reactions harvest energy from simple carbohydrates.3. Distinguish enzymes and subtrates, describe the mechanism enzymes action in relation to energy of activation and active site.1. Define optimum pH and temperature of an enzyme.2. How do changes in pH and temperature affect the native conformation of an enzyme?
- NO AI GENERATED RESPONSE I NEED EXPERTS!! using results for experiment below conduct 1 graph of the different factors vs rate of enzyme activity. * *NO FUNNEL GRAPHS ACTUAL GRAPH WITH GOOD TITLE , AND MAKE SURE IT LOOKS LIKE THE IMAGE I PLACED BELOW** important info: experiment procedure: The experiment began by preparing a hot water bath by boiling water and an ice water bath using ice in a 400 mL beaker. In the control group, 2 mL of 3% H2O2 was placed in a test tube and a pinch of MnO2 was added. The rate of this reaction was assigned as 5, and the production of bubbles in millimeters (mm) was noted. The reaction was considered complete when no more bubbles were produced. Another control group was set up by placing 2 mL of 3% H2O2 in a test tube and adding a pinch of sand, with the rate of reaction assigned as 0. To investigate the difference between plant and animal catalase, 2 mL of H2O2 was added to a test tube and a small piece of fresh liver was added. The rate of…Discuss how enzymes make life possible from a biochemical perspective. Include activation energy barrier,rate of reaction,metabolic regulation, substrate specificity and spontainity of reactionQ: The activation of allosteric enzymes leads to: a) dissociation of protomers upon breaking weak bonds b) hydrolysis of peptide bonds c) phosphorylation of enzyme molecules d) cooperative interaction of subunits e) chemical modification of the enzyme
