nem 14Part C - Comparing and Contrasting the Two Types of Voltage-Gated Ion ChannelsSort the phrases into the appropriate bins depending on whether they describe similarities or differences between voltage-gated K* channels and voltage-gated Na+channels.► View Available Hint(s)Reset HelpThe stimulus that triggers openingThe direction of ion movementthrough the channelThe polarity of the substances theytransport across the membraneSimilaritiesThe placement of the channel proteinrelative to the membraneThe inactivation mechanismDifferences

Answered: Image /qna-images/answer/5de4da67-b557-47f6-b692-5d8b4b349173.jpg

Part C - Comparing and Contrasting the Two Types of Voltage-Gated lon Channels Sort the phrases into the appropriate bins depending on whether they describe similarities or differences between voltage-gated K* channels and voltage-gated Na+ channels. View Available Hint(s) Reset Help The direction of ion movement The stimulus that triggers opening The polarity of the substances they transport across the membrane through the channel Similarities The placement of the channel protein relative to the membrane The inactivation mechanism Differences

Part C - Comparing and Contrasting the Two Types of Voltage-Gated lon Channels Sort the phrases into the appropriate bins depending on whether they describe similarities or differences between voltage-gated K* channels and voltage-gated Na+ channels. View Available Hint(s) Reset Help The direction of ion movement The stimulus that triggers opening The polarity of the substances they transport across the membrane through the channel Similarities The placement of the channel protein relative to the membrane The inactivation mechanism Differences

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

6. What is the instantaneous reaction rate for an enzyme system? k = 0.087 1/h; enzyme concentration = 0.02 M; substrate concentration = 0.05 M; and Km concentration = 0.01 M? Answer should be in units of mM/h
Two-dimensional gel electrophoresis of proteins in a cell extract provides a qualitative way to compare proteins with respect to intracellular abundance. Describe a quantitative approach to determine the number of molecules of an enzyme per cell.
Please study the table. Given the data collected for an enzyme-catalyzed reaction, what is the approximate KM for this enzyme? ISI mM Vo (umol/min) 8 x 10 80 2 x 10 140 8x 10-5 224 4 x 10 3 277 2x 10 2 280 1x 10- 279 2x10 mM 140 umol/min 280 jamol/min 2x 10 mM 98x10mM
2) Given silver oxalate (Ag2C2O4 KSP = 5.40 x10-12) and silver phosphate (Ag3PO4 KSP = 8.89 x10-17) whichsubstance has a greater concentration of the Ag+ ion?
For each of the following statements about ion channels and transporters determine if they are true (T) or false (F). A) lon channels are saturable and transporters are not. SellectJ B) Transporters are saturable and ion channels are not. I Select C) Rates of movement through ion channels are much greater than rates through transporters. [ Select ] D) lon channels and transporters are integral membrane proteins. Select]
Chemistry 3.Calculate the amount of free energy required (or released) to allow electron transport in the ETC to be spontaneous from NADH to ubiquinone under standard conditions based on two electrons moving through the system. This occurs at 25°C. ½ O2 + 2e + 2H+ ® H2O E°´ = 0.815 V NAD+ + 2e +H+ ® NADH E°´ = -0.315 V NADP+ + H+ + 2e ® NADPH E°´ = -0.320 V FAD + 2e +2H+ ® FADH2 E°´ = -0.219 V Ubiquinone + 2H + 2e ® Ubiquinol E°´ = 0.045 V
Trypsin is a serine protease that has a KM of 15 mM. At an initial substrate concentration of 250 µM insulin, trypsin is found to degrade insulin at a rate of 0.6 µM/min. If the concentration of trypsin in solution was 4.326 µM, what is the kcat of trypsin in s-1?
vo(pM/min) 100 90 80 70 60 50 40 30, 20 10 0 What is V max for this enzyme ? Enzyme concentration 0.1 µM 5 10 15 20 A. 100 mm/min B. 1.0 mM/min C. 0.5 μM/min D. 50 µM/min E. 90 µM/min 25 30 35 37
9. Describe the binding between an irreversible inhibitor, such as arsenic, and an enzyme. 10. Explain the difference between reversible competitive and noncompetitive inhibition.
Question 20 What type of inhibition can be reversed? (Select all that apply) Suicide Uncompetitive Competitive Noncompetitive
Given the following data for an enzyme-catalyzed reaction. Substrate conc., mM Velocity, mM/s 0.10 0.96 o.125 1.12 0.167 1.35 0.250 1.66 0.50 2.22 1.00 2.63 1.Write the equation of the line consistent with the Lineweaver- Burke equation (type answer in this format: y=mx+b) 2. Calculate the Vmax. 3. Calculate the Km. Please help me. Kindly explain step by step the solution to this problem. Thank you.