Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
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Chapter 10, Problem 41P
Interpretation Introduction
Interpretation:
The mechanism for phosphorylation of a serine residue from ATP catalysis by protein kinase is to be stated.
Concept introduction:
The organic compounds that contain
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The figure shows the number of cells that have clusters of IRE1 molecules after those cells are treated with various levels of thapsigargin (Tg), a chemical that can induce ER stress. IRE1 can form these clusters when ER stress is induced and this clustering can cause activation of RNAse activity in IRE1. In this experiment, normal IRE1 was used (IRE1α) that can bind to Sec61, along with a modified version of IRE1 that binds to Sec61 more weakly than normal IRE1 (wIRE1α), and another modified version that binds to Sec61 more strongly than normal IRE1 (sIRE1α). From this figure you can conclude that:
Question 18 options:
IRE1 binding to Sec61 promotes the formation of IRE1 clumps
IRE1 binding to Sec61 prevents the formation of IRE1 clumps
co-translational translocation is a key process
the golgi aparatus is heavily involved in the unfolded protein response
The…
SIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met).
Catalase with H2N-...KERINGKERIANGEKSAMSKL-COOH
What is the name of the specific receptor of this polypeptide?
The receptor may also have what alternative function?
TPA protein function. Use at least two sentences to describe the function of the TPA protein.
Chapter 10 Solutions
Biochemistry
Ch. 10 - Prob. 1PCh. 10 - Prob. 2PCh. 10 - Prob. 3PCh. 10 - Prob. 4PCh. 10 - Prob. 5PCh. 10 - Prob. 6PCh. 10 - Prob. 7PCh. 10 - Prob. 8PCh. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - Prob. 11PCh. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - Prob. 15PCh. 10 - Prob. 16PCh. 10 - Prob. 17PCh. 10 - Prob. 18PCh. 10 - Prob. 19PCh. 10 - Prob. 20PCh. 10 - Prob. 21PCh. 10 - Prob. 22PCh. 10 - Prob. 23PCh. 10 - Prob. 24PCh. 10 - Prob. 25PCh. 10 - Prob. 26PCh. 10 - Prob. 27PCh. 10 - Prob. 28PCh. 10 - Prob. 29PCh. 10 - Prob. 30PCh. 10 - Prob. 31PCh. 10 - Prob. 32PCh. 10 - Prob. 33PCh. 10 - Prob. 34PCh. 10 - Prob. 35PCh. 10 - Prob. 36PCh. 10 - Prob. 37PCh. 10 - Prob. 38PCh. 10 - Prob. 39PCh. 10 - Prob. 40PCh. 10 - Prob. 41P
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- Frog poison. Batrachotoxin (BTX) is a steroidal alkaloid from the skin of Phyllobates terribilis, a poisonous Colombian frog (the source of the poison used on blowgun darts). In the presence of BTX, Na+Na* channels in an excised patch stay persistently open when the membrane is depolarized. They close when the membrane is repolarized. Which transition is blocked by BTX?arrow_forwardSIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Protease with mannose-6-phosphate Where is the receptor for this protein located? Where is the final destination of this polypeptide? What happens to the receptor after protein transport?arrow_forwardPlease help me with this question. More than one answer may be correct. THe graph relating to the information is included below. The above figures show the rate of actin polymerization in the presence of various concentration of profilin (Pfn). In the top figure, flourescence intensity is a measure of total actin that has been polymerized, and this is plotted versus time in seconds. The shade of blue of the lines in the top figure correspond to the shaded blue bars representing various concentrations of profilin in the lower figure. The lower graph shows the initial rates of polymerization of actin plotted again concentration. Which of the following is true: Question 21 options: profilin in a molecular motor profilin is a promoter of actin polymerization profilin replaced G-actin in an F-actin strand and breaks the filament profilin is an inhibitor of actin polymerization profilin binds to G-actin, preventing it from polymerizingarrow_forward
- Please help. Both images are connected so this is one question just a part a and b.arrow_forward1G. Please help me in detail. For Molecular Mechanism of ATP versus GTP selectivity of adenylate kinase, Write an expression for the reaction velocity.arrow_forwardNeed help. Plz explain briefly Describe in detail with the aid of diagrams the use of chemical shift perturbation mapping to identify ligand binding sites on a protein.arrow_forward
- Need help. A protein X binds Ligand Y. The kon characterizing this binding is 1 x 106 M-1s-1, koff is 2 x 10-3 M-1s-1. In your in vitro X-Y binding experiment, at what concentration of Ligand Y half of the Protein X would be bound to Y. Assume that the binding is according to the Lock-and-key modelarrow_forwardILLUSTRATIONS. For each of the given proteins: Draw the final location of the following proteins after being translocated. • Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. • Label the amino and carboxyl ends of the protein. Below your drawing, indicate: a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none A. Peroxisome: Class I PMP H₂N- ITS* *Internal targeting sequence -COOHarrow_forwardCell signaling. The ER doctors gave a patient an injection of epinephrine to increase his heart rate and blood pressure. The heart rate and blood pressure went up but not enough. The second dose of the same drug seemed not to have an effect. What do you think may be a possible explanation for this result?arrow_forward
- Inducers and Inhibitors of AEP. Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…arrow_forwardPlease don't copy. Give me correct answer.arrow_forwardILLUSTRATIONS. For each of the given proteins: Draw the final location of the following proteins after being translocated. Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. Label the amino and carboxyl ends of the protein. • Below your drawing, indicate: a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none A. Mitochondrion H₂N- MTS ITS* *Internal targeting sequence that has no cleavage site -COOHarrow_forward
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