Certain enzymes catalyze the covalent linkage of an acetyl group to lysine amino acids as shown below.When a particular target protein is in the un-acetylated state, its interacting partner protein will not bind. However,once acetylated, the partner protein can bind to this target protein.Which of the following can you conclude? Select all that applyCHCONH3.NHLysineacetylationreactionCH,CH,+HaN -C- CO-H.HIN-C- Co-H.UAcetylation changes the secondary structure of the target proteinThe partner protein has acidic residues in the interacting regionAcetylation changes the tertiary structure of the target proteinThe partner protein has basic residues in the interacting region8-1-8-8-8–8–d=

Options 3 and 4 are correct. Acetylation changes tertiary structure of protein and partner protein…

Certain enzymes catalyze the covalent linkage of an acetyl group to lysine amino acids as shown below. When a particular target protein is in the un-acetylated state, its interacting partner protein will not bind. However, once acetylated, the partner protein can bind to this target protein. Which of the following can you conclude? Select all that apply CO NH NH CH, Lysine acetylation reaction CH, CH, +HaN -C- COO- H. HIN -C- CO- HA Acetylation changes the secondary structure of the target protein The partner protein has acidic residues in the interacting region Acetylation changes the tertiary structure of the target protein The partner protein has basic residues in the interacting region

Certain enzymes catalyze the covalent linkage of an acetyl group to lysine amino acids as shown below. When a particular target protein is in the un-acetylated state, its interacting partner protein will not bind. However, once acetylated, the partner protein can bind to this target protein. Which of the following can you conclude? Select all that apply CO NH NH CH, Lysine acetylation reaction CH, CH, +HaN -C- COO- H. HIN -C- CO- HA Acetylation changes the secondary structure of the target protein The partner protein has acidic residues in the interacting region Acetylation changes the tertiary structure of the target protein The partner protein has basic residues in the interacting region

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Three different ligands, Ligand Q, Ligand T, and Ligand W, bind to the same protein but with different affinity: The association constant (Ka) for the binding of Ligand Q to the protein is 0.033 nM-1. The fractional saturation (Y) of the protein is 0.20 when the concentration of Ligand T is 1.25 nM. The fractional saturation (Y) of the protein is 0.80 when the concentration of Ligand W is 72 nM. Given this information, Calculate Kd for the binding of each ligand to this protein. Which ligand binds with greatest affinity? Which ligand binds with the lowest affinity?
Which of the following must be true based on the data below for ligand L binding to protein A and to protein B? Choice 1 of 4:Protein A binds at least 2 molecules of ligand L. Choice 2 of 4:The Kd for ligand binding to B is approximately 4 micromolar. Choice 3 of 4:When exposed to ligand L, protein A reaches maximal binding faster than does protein B. Choice 4 of 4:Protein B must adopt at least 2 different conformations with different binding affinities.
Which of the following situations would produce a Hill plot with nH < 1.0? Explain your reasoning in each case.(a) The protein has multiple subunits, each with a single ligand-binding site. Binding of ligand to one site decreases the binding affinity of other sites for the ligand.(b) The protein is a single polypeptide with two ligand-binding sites, each having a different affinity for the ligand.(c) The protein is a single polypeptide with a single ligand-binding site. As purified, the protein preparation is heterogeneous, containing some protein molecules that are partially denatured and thus have a lower binding affinity for the ligand.
A mutation that changes an alanine residue in the interior of a protein to valine is found to lead to a loss of activity. However, activity is regained when a second mutation at a different position changes an isoleucine residue to glycine. How might this second mutation lead to a restoration of activity?
12 mM of protein A is combined with 6 mM of ligand X in water. After the protein-ligand complex binding reaches equilibrium, you measure that the free ligand concentration is 3 mM and the concentration of protein-ligand complex is 3 mM. What is the Kd for protein A? Although they would be in mM, do not include units in your answer, only the number as a whole integer.
In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys-The hydrophobic residues in this sequence are presented in boldface type.Suggest a possible reason for the periodicity in their spacing.
Histidine is an amino acid with three ionizable groups, one of which has a pKa of 6.0. This group, whenprotonated, has a positive charge. If this ionizable group, within a protein, forms an ionic interaction with anegatively charged group, what would you predict would happen to the pKa of the histidine ionizable group?A. IncreaseB. DecreaseC. Stay the same
Currently, aspartic acid is forming an ionic interaction with arginine in a protein. Part a) If arginine is replaced with glutamic acid, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part b) If arginine is replaced with Lysine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part c) If arginine is replaced with isoleucine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction?
do a and e please and For e, choose two types of interactions, and then give an example of the amino acids in this polypeptide that would interact together in that way.
Consider the following peptide sequence: Lys-Leu-Ile-Cys-Lys What is the net charge of this sequence at physiological pH? a. -2 b. +1 c. 0 d. -1 e. +2
What is the most consistently (i.e. found in every case) energetically unfavorable aspect of protein folding? Does it involve ΔS or ΔH? And what is the most consistently favorable aspect? Again, ΔS or ΔH?
Which of the following is an example of an unacceptable missense? a. HbA is converted to Hb Hikari, where the beta chain Lysine at #61 is replaced by Asparagine. b. Hb A, is converted to Hb M (Boston) where the alpha chain Histidine at #58 is replaced by Tyrosine. c. Hb A is converted to Hb S, where the beta chain Glutamate at #6 is replaced by Valine.