Match the colour of myoglobin to the ligand bound.brownredpink1. carbon monoxide2. nitric oxide3. water

Muscle tissue contains a protein called myoglobin, which is essential for storing and transferring…

Answered: Match the colour of myoglobin to the…

Human Biology (MindTap Course List)

11th Edition

ISBN:9781305112100

Author:Cecie Starr, Beverly McMillan

Publisher:Cecie Starr, Beverly McMillan

Chapter8: Blood

Section: Chapter Questions

Problem 3RQ

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Part B. Myoglobin Final Structure Tertiary or Quaternary Oxygen Binding Affinity Curve is Hyperbolic or Sigmoidal Does it have a heme prosetic group that biinds to oxygen Is it suited for oxygen transport or storage Does is participate in cooperative binding?
Which of these occur when hemoglobin releases oxygen? Select all that apply. O Conformation is shifted toward the T-state BPG can bind in the central channel O Fe2+ is at the center of a planar heme group
In 1913, Archibald Hill described an alternative formulation for cooperative processes such as the binding of oxygen by hemoglobin by considering the hypothetical equilibrium Hb+ n0₂ Hb(0₂)n 2 Analysis leads to the Hill equation: n p02₂" ( Y log (₁ x x ) = log Y (^_^) log where Y is the fractional saturation. This equation suggests that a plot of log with slope n. Plots for myoglobin and hemoglobin are shown here: 3 2 1 O -1 -2 -3 P50 + n = nlog (pO,) – n log(P5o) Myoglobin (0.25, -0.25) -1 0 1 2 log (pO₂) (3.0, 2.5) 3 4 (^_^) log 3 2 1 O -1 -2 -3 -4 (0, -3.4) -1 0 Y Y versus log (pO₂) should yield a line Hemoglobin (2.1, 2.5) - (0.7, -2.0) (1.9, 1.3) (0.4, -3.5) 1 2 log (pO₂) - (2.4, 2.4) 3 4
Which of the following statements is correct of BOTH haemoglobin and myoglobin? Acidic conditions increase the affinity for oxygen. The iron atom of the heme prosthetic group is bound to nitrogen atoms at five of six coordination sites. Four oxygen molecules bind to each subunit. Quaternary structure is found in both haemoglobin and myoglobin. Both haemoglobin and myoglobin show the same oxygen binding affinity at different
Which five statements about hemoglobin and myoglobin structure are true? Each iron atom can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Molecular oxygen binds reversibly to Fe²+ in heme. Heme is composed of an organic protoporphyrin component and a metal atom. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron atom. Each hemoglobin or myoglobin molecule can bind four oxygen molecules. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron atom.
Which of the following is incorrect about 2,3-bisphosphoglycerate (BPG)? It is highly (-) charged b. It prevents binding of O₂ to hemoglobin Oc. It binds only to the relaxed (oxy) conformation of hemoglobin Od. It binds in the space between the four subunits of hemoglobin a.
You are studying with a friend who is describing the Bohr effect. She tells you that in the lungs, hemoglobin binds oxygen and releases hydrogen ion; as a result, the pH increases. She goes on to say that in actively metabolizing muscle tissue, hemoglobin releases oxygen and binds hydrogen ion and, as a result, the pH decreases. Do you agree with her reasoning? Why or why not?
Please answer in full explaination
Myoglobin’s oxygen-binding curve exhibits a shape best described as— serpentine. hyperbolic. straight. sigmoidal. bell.
Which of the following statements regarding the transport of oxygen by hemoglobin is correct? Upon binding of oxygen to heme, a shift in the position of the distal His ultimately induces the switch from T to R states When fully bound to oxygen, AG(R-state)
Select all answers that a

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Match the colour of myoglobin to the ligand bound. brown red pink 1. carbon monoxide 2. nitric oxide 3. water