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

Sickle cell anemia is caused by—     a mutation in a cell surface receptor.     malfunction of an ion channel.     a mutation in the beta subunit of hemoglobin.     deficiency of foliate and iron.     none of the above.

Which statement is true for the heme group present myoglobin:     a. Oxygen binding to heme group is influenced by serine residues within proteins’ sequences.     b. Oxygen binding to heme can become irreversible as a result of interaction with certain protein residues.     c. Oxygen reversibly binds to the heme prostetic group and this binding is influenced by histidine residues within the myoglobin sequence.     d. The heme group dissociates from Mb after oxygen is released.

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

The S protein of SARS-COV-2 binds to a receptor in the Skin called lipid mediated binding factor Lung lining called aveoli expanding factor Nasal epithelium called angiotensin converting enzyme 2 Blood called hemoglobin aggregating factor

Choose all the correct answers for oxygen carrying proteins

what is main difference between myoglobin and hemogloin and in what situations/circumstancees are each used and why?

Which of the following statements does NOT apply to the K value in the equation for the oxygen binding curve of myoglobin? It is numerically equal to p50. O A. It is defined as that oxygen partial pressure at which half of the oxygen binding sites are occupied. В. If Y> K, then myoglobin is less than 50% saturated with oxygen. OC. O D. It is a measure of the affinity of myoglobin for oxygen. OE. It is the value of po2 at which Y = 0.5.

Following several days at high altitude the body responds to the decreased oxygen content of the atmosphere by increasing the amount of 2,3-bisphosphoglycerate it produces. Based on this information and refering to the graph below, identify the correct response from the options. Y (fraction saturation) 1.0 0.8 0.6 0.4 0.2 0.0 0 20 Oxygen Binding plot 40 60 p02 (torr) 80 100 A) Curve y=high altitude and gives a greater release of oxygen to the tissues B) Curve x = high altitude and gives a greater release of oxygen to the tissues C) Curve y=high altitude and allows more oxygen to be bound at low oxygen levels D) Curve x = high altitude and allows more oxygen to be bound at low levels

Why does release of BPG in the blood system help counter the effects of high altitude induced hypoxia? O BPG binds each hemoglobin tetramer and leads to formation of a confirmation that binds 02 more strongly allowing uptake of 02 in the lungs BPG binds myoglobin and leads to formation of a confirmation that binds 02 more strongly allowing uptake of O2 in the lungs BPG binds myoglobin and leads to formation of a confirmation that binds 02 more weakly allowing release of 02 in oxygen starved tissues O BPG binds each hemoglobin tetramer and leads to formation of a confirmation that binds 02 more weakly allowing release of 02 in oxygen starved tissues