BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
9th Edition
ISBN: 9781319425784
Author: BERG
Publisher: Macmillan Higher Education
expand_more
expand_more
format_list_bulleted
Question
Chapter 18, Problem 49P
Interpretation Introduction
Interpretation:
Electroneutral exchange of H2PO4- for OH- is the same as electroneutral symport of H2PO4- and H+.
Concept introduction:
In the majority of inner membrane carriers, antiport transport occurs. Antiport transport is the process in which the exchange of one molecule for the other molecule occurs. On the other hand, symport transport is the transfer of molecules in the same direction. The charge differences in the antiport and symport transport will result inthe electrical transport process.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
More ratios. Through the use of nuclear magnetic resonance
spectroscopy, it is possible to determine the ratio between the
protonated and deprotonated forms of buffers. (a) Suppose the ratio
of [ A- ]A I to [HA] is determined to be 0.1 for a buffer with
pKar6.0.pKa = 6.0. What is the pH? (b) For a different buffer,
91974
suppose the ratio of [ A- ]lA J to [HA] is determined to be 0.1 and
the pHpH is 7.0. In this case, what is the pKapKa of the buffer? (c) For
another buffer with pKa=7.5PKa = 7.5 at pH 8.0pH 8.0, what is the
expected ratio of [ A- ][A ] to [HA]? do
The number 2 question. Thank you
I don't understand it. Can u help me? Can u help me to explain this to me, please
Chapter 18 Solutions
BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
Ch. 18 - Prob. 1PCh. 18 - Prob. 2PCh. 18 - Prob. 3PCh. 18 - Prob. 4PCh. 18 - Prob. 5PCh. 18 - Prob. 6PCh. 18 - Prob. 7PCh. 18 - Prob. 8PCh. 18 - Prob. 9PCh. 18 - Prob. 10P
Ch. 18 - Prob. 11PCh. 18 - Prob. 12PCh. 18 - Prob. 13PCh. 18 - Prob. 14PCh. 18 - Prob. 15PCh. 18 - Prob. 16PCh. 18 - Prob. 17PCh. 18 - Prob. 18PCh. 18 - Prob. 19PCh. 18 - Prob. 20PCh. 18 - Prob. 21PCh. 18 - Prob. 22PCh. 18 - Prob. 23PCh. 18 - Prob. 24PCh. 18 - Prob. 25PCh. 18 - Prob. 26PCh. 18 - Prob. 27PCh. 18 - Prob. 28PCh. 18 - Prob. 29PCh. 18 - Prob. 30PCh. 18 - Prob. 31PCh. 18 - Prob. 32PCh. 18 - Prob. 33PCh. 18 - Prob. 34PCh. 18 - Prob. 35PCh. 18 - Prob. 36PCh. 18 - Prob. 37PCh. 18 - Prob. 38PCh. 18 - Prob. 39PCh. 18 - Prob. 40PCh. 18 - Prob. 41PCh. 18 - Prob. 42PCh. 18 - Prob. 43PCh. 18 - Prob. 44PCh. 18 - Prob. 45PCh. 18 - Prob. 46PCh. 18 - Prob. 47PCh. 18 - Prob. 48PCh. 18 - Prob. 49PCh. 18 - Prob. 50PCh. 18 - Prob. 51PCh. 18 - Prob. 52PCh. 18 - Prob. 53PCh. 18 - Prob. 54PCh. 18 - Prob. 55PCh. 18 - Prob. 56PCh. 18 - Prob. 57PCh. 18 - Prob. 58PCh. 18 - Prob. 59P
Knowledge Booster
Similar questions
- Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?arrow_forwardBe sure to answer all parts. Calculate the equilibrium constants for decomposition of the following hydrogen halides at 298 K. Enter your answers in scientific notation. (a) 2HF(g) H2(g) + F2(g) 0.5 x 10 -97 (b) 2HCl(g) H2(g) + Cl2(g) 3.8 LOL -34 (c) 2HBr(g) H2(g) + Br2(g) 4.9 LO -20 (d) 2HI(g) H2(g) + I2(g) 1.1 -3arrow_forward6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?arrow_forward
- Balance the reactions. A hint is provided to help you decide if the reaction will proceed as written, ie from left to right. Do not leave any fractions. 1. a) Balance Al₂O3 → Al + 0₂ b) What type of reaction is this? c) Is this a redox rx, yes / no ? d) The reaction will go from left to right, yes / no ? (hint: O₂ is very reactive) 2. a) Balance HNO3 + AI → b) What type of reaction is this? c) Is this a redox rx, yes / no ? d) The reaction will go from left to right, yes / no ? (hint: aluminum is a reactive metal, and a gas escapes) C7H14 + 0₂ 3. a) Balance, leave no fractions b) What type of reaction is this? c) Is this a redox rx, yes / no ? d) The reaction will go from left to right, yes / no ? (hint: O₂ is very reactive) H2(g) + AI(NO3)3 → CO₂ + H₂Oarrow_forwardFor 100 words. What are the two essential requirements to effectively carry out metabolic work?arrow_forwardNeed help, please.arrow_forward
- Chemical labeling of chymotrypsin by the compound tosylphenylalanine chloromethyl ketone (TPCK) modifies the His 57 in the enzyme's active site. The structure of this derivative is shown below. TPCK inactivates the enzyme because the bulky addition prevents it from cleaving nearby covalent bonds. HCI + CH, C-O Chymotrypsin-His 57 TPCK Modified enzyme True O Falsearrow_forwardNot too sure if my answer is correct.arrow_forwardGood evening. I hope you are well. My chemistry question is attached to this message as a JPG.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning