Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 36, Problem 16P
Interpretation Introduction
Interpretation:
The mechanism of working of smooth muscles with help of calcium ions should be determined.
Concept introduction:
The smooth muscles are the muscles that work involuntarily. These muscles are not under the influence of the consciousness. They are regulated by the calcium ions and are non-striated.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
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?
Fo-F1 ATPase. The energy for ATP synthesis from ADP and Pi is provided by the downhill transport of protons through the rotary FoF1 ATP synthase . The enzyme has 3 alpha-beta and 12 ‘c’ subunits. The mitochondrion maintains change in membrane potential=180 mV (negative inside), pHin = 8, pHout=7, [Pi] = 3 mM and ADP is present as well.
. What [ATP]/[ADP] ratio will be established at steady-state under these conditions?
What would be the [ATP]/[ADP] ratio if the enzyme had only 9 ‘c’ subunits? full revolution of the crank (gamma subunit) produces 3 ATP.
nerve impulses. Neurotransmitters are packaged by the cell into small, membrane-
bound sacs called vesicles. Upon receiving a chemical signal, the vesicles move
towards the cell membrane and fuse with it, releasing the enclosed
neurotransmitters from the terminal end of the nerve cell. Which organelle is most
likely responsible for packaging neurotransmitters into a vesicle?
Mitochondria
Golgi body
Ribosomes
Nucleus
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Signal transduction pathway. Sketch a G protein in the active and inactive stages, and label its parts.arrow_forwardInducers 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_forwardFo-F1 ATPase. The energy for ATP synthesis from ADP and Pi is provided by the downhill transport of protons through the rotary FoF1 ATP synthase (lecture 22). The enzyme has 3 a-b and 12 ‘c’ subunits. The mitochondrion maintains Df=180 mV (negative inside), pHin = 8, pHout=7, [Pi] = 3 mM and ADP is present as well. How much energy is available (from the proton electrochemical gradient) for ATP synthesis under these conditions (in kJ/mol)? What [ATP]/[ADP] ratio will be established at steady-state under these conditions? What would be the [ATP]/[ADP] ratio if the enzyme had only 9 ‘c’ subunits? Remember that full revolution of the crank (gamma subunit) produces 3 ATP.arrow_forward
- Please help me with this question. PLEase give me the right answer and for number 2 WRITE AT LEAST A PARAGRAPGH and dont copy from internet.arrow_forwardPlease help me with this question. More than one answer may be correct. THe graph relating to the information is included below. 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…arrow_forwardLigand binding and response. The following question involves the ligand binding to a receptor and the receptor's response to that ligand. What ligand concentration would be required for a full agonist with a KD of 8 nM to achieve a response of 0.75?arrow_forward
- 1G. Please help me in detail. For Molecular Mechanism of ATP versus GTP selectivity of adenylate kinase, Write an expression for the reaction velocity.arrow_forwardCrohn’s disease. Omega-3 fatty acids have been tested asa means to prevent relapse of Crohn’s disease. Two large,randomized, placebo-controlled studies have shown nosuch benefit from omega-3 fatty acids. Suppose you areasked to design an experiment to further study this claim.Imagine that you have collected data on Crohn’s relapsesin subjects who have used these omega-3 fatty acids and similar subjects who have not used them and that you canmeasure incidences of relapse for these subjects. Statethe null and alternative hypotheses you would use in yourstudy.arrow_forwardNeed help, please. I know the answer isn't mitotic spindle or secretory and endocytic vesicle transport. I think the answer is option C, axon stiffening, and neurotransmitter vesicle transport, but I am not 100% sure. What function of the microtubule motor proteins dynein and kinesin is blocked by the use of colchicine to treat gout? Select one: O a. mitotic spindle b. secretory and endocytic vesicle transport c. axon stiffening and neurotransmitter vesicle transport O d. ER, Golgi, and mitochondria movementarrow_forward
- No plagiarism please. Use your own words. Thanks. Discuss the preferred locations of different classes of amino acids in transmembrane proteins. Explain the formation of thioether-linked prenyl anchor proteins. Explain the structure of caveolae.arrow_forwardIDENTIFICATION. One of the B-complex vitamins which is the precursor of Nicotinamide in the coenzyme NAD+. Carrier of the activated amino acids to the ribosomes for incorporation into the growing peptide chain. Molecule that attaches to myosin and actin during muscle contraction.arrow_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
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY 
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON