Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 7, Problem 16P
An antibody has been isolated that binds to F-actin but not to G-actin. What structural feature (s) of F-actin do you suppose the antibody binds (i.e., how is the antibody able to distinguish between these two forms of actin)?
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A group of researchers have isolated three novel compounds from the venom of a newly discovered species of wasp. Based on their structure and protein chemistry, the researchers believe that all three compounds may have strong anti-inflammatory activity and they have devised an experiment to test whether their compounds can reduce muscle damage after exercise. They plan to induce muscle damage in mice by causing repeated eccentric contractions (by running them downhill on a treadmill), and then examine the amount of inflammation in the muscles of their mice 24hrs later. They will use the following treatment groups:
Sample 1) no treatment (control)
Sample 2) 1mg/kg of Compound ‘A’
Sample 3) 1mg/kg of Compound ‘B’, and;
Sample 4) 1mg/kg of Compound ‘C’.
They perform their experiment and analyse their results using ANOVA followed by a post-hoc test. The results are as follows: (IMAGE ATTCAHED)
QUESTION IS: Having selected which of their compounds seems the most promising, the…
2) After plotting actin bound to cofilin versus the cofilin concentration, you generate the
figure below.
v (cofilin binding density)
1
0.8
0.6
0.4
0.2
0
2
4
6
8
[S. pombe cofilin] free (UM)
10
a) What is the Kd you measure for this
interaction?
b) What is the AG of the interaction?
c) Based on the data, is there anything you
suspect about the binding of protein and
ligand?
The Structure of the acetylcholine receptor is shown below:
A. Knowing the amino acid sequence of this protein, what tool would you use to identify the membrane-spanning region? Explain how it works.
Chapter 7 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 7 - Prob. 1PCh. 7 - Certain antibodies have been shown to bind only to...Ch. 7 - Antibodies raised against a macromolecular antigen...Ch. 7 - Prob. 4PCh. 7 - Prob. 5PCh. 7 - Prob. 6PCh. 7 - Prob. 7PCh. 7 - Prob. 8PCh. 7 - Prob. 9PCh. 7 - Prob. 10P
Ch. 7 - Prob. 11PCh. 7 - Prob. 12PCh. 7 - Prob. 13PCh. 7 - Suppose your biking partner claims that...Ch. 7 - Prob. 15PCh. 7 - An antibody has been isolated that binds to...Ch. 7 - A typical relaxed sarcomere is about 2.3 m in...Ch. 7 - Each gram of mammalian skeletal muscle consumes...Ch. 7 - A few hours after the death of an animal, the...
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- α-Bungarotoxin is a powerful neurotoxin found in the venom of a poisonous snake (Bungarus multicinctus). It binds with high specificity to the acetylcholine receptor (AChR; an integral membrane protein) andprevents its ion channel from opening. This interaction was used to purify AChR from the electric organ of torpedo fish.(a) Outline a strategy for using α-bungarotoxin covalently bound to chromatography beads to purify the AChR protein. (b) Outline a strategy for the use of [125I]α-bungarotoxin to purify the AChR protein.arrow_forwardLigand binding to proteins may occur with varying strengths; some ligands bind tightly to proteins while others bind less tightly. The strengths of reversible binding are determined experimentally by varying concentrations of ligands, and measuring the saturation of the protein in the various ligand concentrations. One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below: 1) Provide a brief explanation as to why ligand binding to proteins must be a reversible process. 2) Calculate the dissociation constant (Kd) for the hormone binding to each of the three proteins.arrow_forwardInhibitors of acetylcholinesterase, such as edrophonium, are used to treat Alzheimer’s disease. The substrate for acetylcholinesterase is acetylcholine. Structures are attached. What kind of inhibitor is edrophonium? Explain. Can inhibition by edrophonium be overcome in vitro by increasing the substrate concentration? Explain. Does this inhibitor bind reversibly or irreversibly to the enzyme? Explain.arrow_forward
- Amoeboid cells that migrate through our tissues, such as the class of white blood cells known as neutrophils, often do so in a directed manner, triggered, for instance, by chemical signals released by pathogens such as bacteria. Directed migration in response to a chemical stimulus is known as chemotaxis. Part of an efficient chemotactic response is the ability of cells to polarize. As is the case with our structurally-polar polymers like F-actin or microtubules, polarization here refers to an asymmetry in the cells, rather than an electrical charge. In this case, it involves one part of the cell becoming the “front” (or leading edge) and another the rear. In a well-polarized, migrating cell, it’s been observed that an active form of Rac (which, in turn, can activate ARP 2/3) is concentrated towards the front of the cell, whereas an active form of Rho (which, in turn, can activate formin, inhibit cofilin/ADP, and activate myosin II) is found toward the rear of the cell. Based on your…arrow_forwardAmoeboid cells that migrate through our tissues, such as the class of white blood cells known as neutrophils, often do so in a directed manner, triggered, for instance, by chemical signals released by pathogens such as bacteria. Directed migration in response to a chemical stimulus is known as chemotaxis. Part of an efficient chemotactic response is the ability of cells to polarize. As is the case with our structurally-polar polymers like F-actin or microtubules, polarization here refers to an asymmetry in the cells, rather than an electrical charge. In this case, it involves one part of the cell becoming the “front” (or leading edge) and another the rear. In a well-polarized, migrating cell, it’s been observed that an active form of Rac (which, in turn, can activate ARP 2/3) is concentrated towards the front of the cell, whereas an active form of Rho (which, in turn, can activate formin, inhibit ADP, and activate myosin II) is found toward the rear of the cell. Based on your…arrow_forwardWhich 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.arrow_forward
- After death, muscles become very stiff, a condition known as rigor mortis. Explain the molecular basis of rigor mortis - where in the contraction cycle is the muscle arrested? Why?arrow_forward12 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.arrow_forwardWrite schematically the synthesis of phosphatidylcholine from phosphatidylethanolamine. What compounds are necessary for this biochemical process? Biological significance of phospholipids.arrow_forward
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