In biochemistry, the activity of an enzyme is regulated by many factors as in the followings, except Allosteric modulators DNA melting points MRNA stability Dephosphorylation of phosphorylated proteins protein pH environment

In biochemistry, the activity of an enzyme is regulated by many factors as in the followings, except Allosteric modulators DNA melting points MRNA stability Dephosphorylation of phosphorylated proteins protein pH environment

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 22QP: Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant...

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Question

In biochemistry, the activity of an enzyme is regulated by many factors as in the followings, except
Allosteric modulators
DNA melting points
MRNA stability
Dephosphorylation of phosphorylated proteins
protein pH environment

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Allosteric Inhibitors ● are constructed of level of protein polypeptide chains (demonstrating on each polypeptide. structure) with an ● The enzyme moves back and forth between an active state and an inactive state ● If a substance binds to the allosteric site and puts the enzyme into the active state, that substance is called an ● If a substance binds to the allosteric site and puts the enzyme into the inactive state, that substance is called
this is not a writing assignment or essay just give a brief explanation
Binding of a ligand to protein X affects the binding properties of another site on X. This is an example of which of the following phenomena? transition state stabilization competitive inhibition noncompetitive inhibition induced fit allosteric regulation
In order to stabilize a protonated Asp amino acid in an active site, an enzyme could: Choose the one best answer. have the Asp located in the hydrophobic core of the protein. O have the Asp located on the exterior of the protein, interacting with the hydrophilic cytoplasm. surround the Asp with negatively charged amino acids. surround the Asp with positively charged amino acids. do nothing: Asp residues are normally protonated at physiological pH.
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List some advantages of phosphorylation/dephosphorylation cascade systems over simple allosteric regulation.
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In any given enzyme, the active site is only a small portionof the entire molecule. Synthesis of such a relatively largemolecular machine requires an enormous amount of cellular energy. Explain why this inefficiency is tolerated.
Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.
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The blue structure in the diagram below is an enzyme. Please discuss what these diagrams (A and B) show. Please explain whether the grey tube within the enzyme would be effective as a drug or medication to inhibit this enzyme in both A and B. What type of drug or medication would this be called? A B ( ES ES OO #