The allosteric site 1). Draw a representation of an allosteric binding site of an enzyme. must bind an allosteric modifier that maintains three hydrophobic regions, a polar charged region and two regions of hydrogen bonding. You choose the order or organization of the characteristics in the allosteric site - label all regions. Details - the allosteric site is composed of faces of two separate beta sheets and two separate alpha helices. You might decide that each beta sheet or each alpha helix contributes one amino acid R group to the allosteric site or you may decide that one of the beta sheets or one of the alpha helixes contributes two or more amino acid R groups to the allosteric organization. Your choice but please show R group structure in the allosteric site!

The allosteric site 1). Draw a representation of an allosteric binding site of an enzyme. must bind an allosteric modifier that maintains three hydrophobic regions, a polar charged region and two regions of hydrogen bonding. You choose the order or organization of the characteristics in the allosteric site - label all regions. Details - the allosteric site is composed of faces of two separate beta sheets and two separate alpha helices. You might decide that each beta sheet or each alpha helix contributes one amino acid R group to the allosteric site or you may decide that one of the beta sheets or one of the alpha helixes contributes two or more amino acid R groups to the allosteric organization. Your choice but please show R group structure in the allosteric site!

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter25: Nitrogen Acquisition And Amino Acid Metabolism

Section: Chapter Questions

Problem 9P

See similar textbooks

Similar questions

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.
Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
Understanding the Nature of the Ubiquitin-Ubiquitin linkage Draw the structure of the isopeptide bond formed between Gly76of one ubiquitin molecule and Lys48of another ubiquitin molecule.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
Amino acids have the generic structure seen below, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
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 pieces
Energetic of Fructose-1 ,6-bis P Hydrolysis (Integrates with Chapter 3.) The standard free energy change (G) for hydrolysis of fructose-1. 6-bisphosphate (FBP) to fructose-S-phosphate (F-6-P) and P: is -16.7 KJ/mol: FBP + H2O fructose-6-P + Pi The standard free energy change (G) for ATP hydrolysis is -30.5 KJ/mol: ATP + H2O ADP + Pj What is the standard free energy change for the phosphofructokinase reaction: ATP + fructose-6-P ADP + FBP b. What is the equilibrium constant for this reaction? c. Assuming the intracellular concentrations of [ATP] and (ADP] are maintained constant at 4 mM and 1.6 mM, respectively, in a rat liver cell, what will be the ratio of [FBP]/[fructose-6-P] when the phosphofructokinase reaction reaches equilibrium?
Amino acids are not stored in the body. Describe how excess amino acids are processed in the cell.
Exploring the Structure of the 30S Ribosomal Subunit Go to www.pdh.org and bring up PDB file 1GIX, which shows the 30S ribosomal subunit, the three tRNAs, and mRNA. In the box on the right titled â€˜Biological Assembly.â€� click â€œMore Images.â€� and then scroll down to look at the Interactive Vic By moving your cursor over the image, you can rotate it to view it from any perspective. a. How are the ribosomal proteins represented in the image? b. How is the 16S rRNA portrayed? c. Rotate the image to see how the tRNAs stick out from the structure. Which end of the tRNA is sticking out? d. Where will these ends of the tRNAs lie when the 50S subunit binds to this complex?
If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work?
Explain what happens if even one amino acid is substituted for another in a polypeptide chain. Provide a specific example.