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 2P
Interpretation Introduction
Interpretation:
The body length per second of the kinesin molecules and the automobile of 10feet long at the given rate should be compared.
Concept introduction:
The kinesin is a class of motor protein in eukaryotic cells. They are powered by the ATP molecules in the cells and they move along the microtubule filaments.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
A healthy 32-year-old man lifts weights regularly as part of his workout. In one of his biceps muscle fibers at rest, the length of the I band is 1.0 μm and the A band is 1.5 μm. Contraction of that muscle fiber results in a 10% shortening of the length of the sarcomere. What is the length of the A band after the shortening produced by muscle contraction? Draw the sarcomere before and after contraction.
Avidin exists as a protein complex of around 68 kDa. Research to determine the types of interactions that hold the avidin complex together.
Based on your research, which molecular weight would you expect for avidin when treated with beta-mercaptoethanol and run through a native gel?
35 kDa
68 kDa
10 kDa
19 kDa
When you hold a weight at arm's length, you are not doing any thermodynamic work but the muscles supporting the weight are nevertheless consuming energy. Describe, on the molecular level, how muscles might maintain such state of constant tension without contracting. Why does this state consume ATP?
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
- is this stement false? Intracellular concentrations in resting muscle are as follows: Fructose-6-phosphate (1.0 mM)Fructose-(1-6)-bisphosphate (10.0 mM)AMP (0.1 mM)ADP (0.5 mM)ATP (5.0 mM)Pi (10.0 mM)Under the above conditions the Phosphofructokinase reaction in muscle is more exergonic than under standard conditions.arrow_forwardThe sarcoplasmic reticulum Ca2+-ATPase, pumps 2 mol Ca2+ out of sarcomeres per mol ATP hydrolyzed.(a) Given the following steady-state concentrations and a membrane potential of 65 mV (inside negative), calculate ΔG for the following activetransport process at 37 °C and pH = 7.4:2Ca2+(in) + ATP + H2O → 2Ca2+(out) + ADP + Pi + H+ATP = 2.6 mM, ADP = 210 μM, Pi = 5.1 mM, Ca2+(in) = 32 mM,Ca2+(out) = 2.2 mM(b) In active muscle the pH can drop below 7.4. Is the reaction above moreor less favorable under these conditions?(c) The activity of the Ca2+-ATPase is regulated reversibly under normalconditions to maintain homeostatic concentrations of Ca2+ inside thesarcomere. However, in a rare genetic disorder, irreversible activation ofthe Ca2+ -ATPase can occur. Assuming 37 °C, pH = 7.4, and the steadystate concentrations for ATP, ADP Pi, and Ca2 +(out) given in part (a),calculate the minimum [Ca2 +] inside a sarcomere that has irreversibly activated Ca2 +-ATPase (i.e., the Ca2 +-ATPase…arrow_forwarddiscuss the four types of attractive forces that give the raise to tertiary proteinstructurearrow_forward
- Chemistry Calculate the fractional saturation of myoglobin at 30 torr (p50=2.8 torr). An allosteric protein has a hill coefficient of 0.4. Which model of Allosterism fails to explain the cooperativity exhibited by this protein? Explain why?arrow_forwardCreate a ROUGH SKETCH (no need for exact hydropathy indices and residue numbers) of the hydropathy plot for the given membrane protein. -coo Please follow the color assignment of the helical domains and properly label the plot and axes. Here is an example: Amino Outside terminus Transmembrane helices are predicted by hydrophobic stretches of 20-25 aa residues 10 50 100 150 200 250 Hydrophobic Inside Hydrophilic Carboxyl terminus -3 10 50 100 150 200 250 Residue number Bacteriorhodopsin Hydropathy indexarrow_forwardRoughly sketch the hydropathy plot for the given hypothetical membrane protein. Follow the color assignment of the helical domains and properly label your plot and axes (NB: Only a rough sketch is being asked. No need be exact with the hydropathy indices and residue numbers). CO-arrow_forward
- You are studying the rate of actin polymerization and depolymerization in an in-vitro hypothetical system. The G actin concentration in the solution of the experimental setup is 0.3μm. Based on the data values predict the outcome of the experiment. Please note that X or Y ends can be "any end" of the actin filament. -1 X end actin: Association rate: 10 µmS-¹ ; Dissociation rate: 2.5 µmS-¹ Y end actin: Association rate: 5 µmS-¹ ; Dissociation rate: 2.5 µmS-¹ O The X end of the actin filament will grow. O Neither X or Y end of the filament will grow. O The Y end of the actin filament will grow. O There is not sufficient data to predict thearrow_forwardFinally, discuss the consequences of 9.2 uM for actin polymerization in a cell, considering critical concentrations values of 0.1 uM for barbed (plus) end addition and 0.6 uM for pointed (minus) end addition of actin. Recall that at G-actin concentrations above the critical concentration, actin filaments elongate. When the G-actin concentration is greater than the Cc for the barbed end (C (T)) but less than the Cc for the pointed end (Cc (D)), the filament maintains a steady state length due to treadmilling, where the rate of ATP actin addition at the barbed end equals the rate of ADP-actin at the pointed end.arrow_forwardWrite the Structure Activity Relationship ( SAR) of Captopril ? Please write at your own words.arrow_forward
- The concentration of actin in cells is 50–100 timesgreater than the critical concentration observed for pureactin in a test tube. How is this possible? What prevents theactin subunits in cells from polymerizing into filaments?Why is it advantageous to the cell to maintain such a largepool of actin subunits?arrow_forward. The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?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_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. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals 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 LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals 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