The shape for curve of oxygen binding to Myoglobin is curve of oxygen binding to Hemoglobin is Flat, Sigmoidal Hyperbolic, Sigmoidal Hyperbolic, Hyperbolic Sigmoidal, Sigmoidal and the shape for
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- The shape for curve of oxygen binding to Myoglobin is ___________ and the shape for curve of oxygen binding to Hemoglobin is _________________ Hyperbolic, Hyperbolic Sigmoidal, Sigmoidal Flat, Sigmoidal Hyperbolic, SigmoidalExplain the operation of the Cori cycle and its importance to muscles. O Focus 目 of 2 190 words 以 W e Type here to search Chp f12 insert fg f9 144 17 16 fs (4 & 6. 00Figure 6 shows the binding of oxygen to myoglobin and haemoglobin (Y-axis: Fraction saturation) when they are exposed to various partial pressures of oxygen (X-axis: pO2). 0.9 0.8 Myoglobin 0.7 0.6 0.5 0.4 Hemoglobin 0.3 0.2 0.1 2 10 12 Po, (kPa) Figure 6 (i) Briefly compare the protein structure of myoglobin to that of haemoglobin. (ii) Based on Figure 6, explain the differences between the functions performed by myoglobin and haemoglobin. Fraction saturation
- Which of the following is the concentration of hemoglobin-bound oxygen in the blood when the heme is fully saturated? 8500 uM 8630 uM 2200 uM 8800 uMOxygen deficit is another term for EPOC True O FalsePlease explain the difference between the oxygen dissociation curve created by myoglobin (asymptotic) versus the oxygen dissociation curve created by hemoglobin (sigmoidal). Why does this occur? Myoglobin O₂ saturation (%) 100 80 60 40 20 0 20 Hemoglobin 40 60 80 100 120 Po₂ (mmHg)
- Select all statements that correctly describe hemoglobin and myoglobin structure. Each hemoglobin molecule can bind four oxygen molecules; each myoglobin can bind one oxygen molecule. Molecular oxygen binds irreversibly to the Fe(II) atom in heme. Each iron atom can form six coordination bonds. One of these bonds is formed between iron and oxygen. Hemoglobin and myoglobin are heterotetramers. The heme prosthetic group is entirely buried within myoglobin. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron (Fe) atom. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron.As the value of p50 myoglobin for oxygen. increases, decreases decreases, increases decreases, decreases increases, increases None of the above the value of K _--_, resulting in a high affinity ofExplain the clinical significance of a right or left shift of the oxyhemoglobin dissociation curve with regard to the loading of oxygen in the lungs and unloading of oxygen at the tissues.
- Describe the clinical significance of the flat portion of the oxyhemoglobin dissociation curve.The dissociation constant is defined by p50 = 2.8 torr for myoglobin binding to oxygen. What is partial pressure of oxygen when half of the myoglobin proteins in solution are bound to oxygen?4.2 Detail the similarities and differences between myoglobin and hemoglobin structure.