Unfortunately, carbon monoxide was not a common molecule when hemoglobin evolved,and the binding site does not distinguish between Oz and Co. When carbon monoxide ispresent, it can bind to some of the available hemoglobin sites, which prevents thehemoglobin from carrying oxygen.Fo*Fe*Fe*B. CO binds at an absorption site with energy €co = -3.45 × 10-20 J. Suppose there is a 1to 100 ratio of CO to O2 present in the blood. For simplicity's sake, assume there are now100 Oz molecules available to bind.1. What are the possible states now, and what are their multiplicities?

The objective of this question is to explain the possible state and multipleties. It show 1:100…

Unfortunately, carbon monoxide was not a common molecule when hemoglobin evolved, and the binding site does not distinguish between O₂ and CO. When carbon monoxide is present, it can bind to some of the available hemoglobin sites, which prevents the hemoglobin from carrying oxygen. Fe² Fe² B. CO binds at an absorption site with energy co= -3.45 x 10-20 J. Suppose there is a 1 to 100 ratio of CO to O2 present in the blood. For simplicity's sake, assume there are now 100 0₂ molecules available to bind. 1. What are the possible states now, and what are their multiplicities?

Unfortunately, carbon monoxide was not a common molecule when hemoglobin evolved, and the binding site does not distinguish between O₂ and CO. When carbon monoxide is present, it can bind to some of the available hemoglobin sites, which prevents the hemoglobin from carrying oxygen. Fe² Fe² B. CO binds at an absorption site with energy co= -3.45 x 10-20 J. Suppose there is a 1 to 100 ratio of CO to O2 present in the blood. For simplicity's sake, assume there are now 100 0₂ molecules available to bind. 1. What are the possible states now, and what are their multiplicities?

Chemistry for Engineering Students

3rd Edition

ISBN:9781285199023

Author:Lawrence S. Brown, Tom Holme

Publisher:Lawrence S. Brown, Tom Holme

Chapter11: Chemical Kinetics

Section: Chapter Questions

Problem 11.61PAE

See similar textbooks

Similar questions

H20 -OH H30* (1) XS LIAIH4 (2) H2O HO, он (1) XS CH;MgBr (2) H20
explain why? • Levofloxacin is a broad spectrum antibotic. It is reported that itis completely removed in an unchanged from the body and itselimination half life is 7 h. Determine the amount oflevofloxacin eliminated in urine at 10 h following IV bolusadministration of 6,25 mg/kg dose to a patient weighing 80 kg.a. 185,75 mgb. 314,25 mgc. 314,25 mg/kgd. 18,57 mg How long will it take to lose 75% of the administered doseof a drug from the body if the drug follows first orderprocess?a. 3,32 half livesb. 2,32 half livesc. 2.0 half livesd. None of the above
Given the reaction of 4 C (s) + 3 H2 (g) + O2 (g) 2 C2H2 OH (1) AH %3D 542 J | What would the AH for 4 C2H2 OH (1) → 8 C (s) + 6 H2 (g) + 2 02 (g) be? O-271 J O 1084 J O 271 J O-1084 J 73°F S
3.25 mL of Biomarker A (4.21 x 10-7 mol L-1) was brought up to volume with deionized water in a 50 mL volumetric flask. What is the final concentration after this dilution (in mol/ L)
If the a and b loci are 16 mu apart in humans and an A B / a b woman marries an a b / a b man. What is the probability that their first child will be A b / a b? 0.08 0.16 0.32 0.84 0.64
Which of the following is the correct Ksp expression for Al2(SO4)3(s)? OKsp [A1³+12[SO4²-1³ = Ksp = [2A1³+][3SO42-1 OKsp = ([A1³+12[SO4²-1³) / [Al2(SO4)3] Ksp [A13+12+ [SO4²-1³ =
A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction The researchers begin to characterize the enzyme. a)In the first experiment, with [Et] at 4 nM, they find that the Vmax is 1.6 μM s-1. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) b)In another experiment, with [Et] at 1 nM and [HAPPY] at 30 μM, the researchers find that V0300 nM s-1. What is the measured Km of happyase* for its substrate HAPPY? (Include appropriate units.) c)Further research shows that the purified happyase* used in the first two experiments wasactually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax in (a) is increased to 4.8 μM s-1, and the measured Km in (b) is now 15 μM. For the inhibitor ANGER, calculate the values of αand α’.
A research group discovers a neW version oI happyasee, which they nappyase", that catalyzes the chemical reaction HAPPY = SAD The researchers begin to characterize the enzyme. In the first experiment, with [E] at 4 nM, they find that the Vmax is 1.6 µM s-1. Based on this experiment, what is the kcat for happyase*? kcat 400 S In another experiment, with [E,] at 1 nM and [HAPPY] at 30 µM, the researchers find that Vo is equal to 300 nM s-1. What i the measured Km of happyase* for its substrate HAPPY? Km 10 x10–6 Incorrect Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax increases to 4.8 µM s-, and the measured Km is now 15 µM. S For the inhibitor ANGER, calculate the values of a' and a. a' 2 Incorrect 2
on O C The u receptors are a class of opioid receptors. The binding affinity of several compounds is shown below: Compound Binding affinity 2.55 nM || ||| IV 33.6 nM 156 nM 600 nM H i. Which compound has the weakest binding to the μ receptor? Justify your answer. ii. Which compound has the strongest binding to the μ receptor? Justify your answer. DJelsim Suppost 2² Tina, me 3 Course Hero' Rewards 2 OSHC Claims (Allian. 7 warded messa N Telsim Prepaid Pack [04933442 invoice and referral - Good morni Good news: you have new rewards o + bly Re-Further information Regi 8 Google recommends Chrome 24℃ 대체로 화창 A 9. 2023
Explain why is FAAS a good method of quantifying Ca in milk?
5. Varying the enzyme- For a one substrate, enzyme-catalyzed reaction, double reciprocal plots were determined for three different enzyme concentrations. Which of the following three families of curve would you expect to be obtained? Explain. Value 1/Vo 1/Vo 1/Vo 1/[S] 1/[S] 1/[S]
N2 (g) + 3 H2 (g) = 2 NH3 (g) + 100 KJ affect on (H2] affect on INH31 disturbance affect on IN2] increase N2] decrease increase increase pressure increase temp