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Homework answers / question archive / Which of the following statements is FALSE regarding the interaction of oxygen with myoglobin? Which of the following occurs in hemoglobin when blood pH is lowered? The binding of one O2 to a molecule of hemoglobin results in: An increased affinity for O2 in the remaining subunits (which have not yet bound O2) Which of the following statements about the T and R states of hemoglobin is FALSE? Which of the following statements is FALSE? Which term best describes the histidine F8 residue in myoglobin and hemoglobin? Which of the following statements about the structure of myoglobin is TRUE? hich of the following statements is FALSE regarding the interaction of oxygen with myoglobin? Which of the following statements about the T and R states of hemoglobin is FALSE?
Oxygen is a homoallosteric effector of myoglobin.
Histidine side chains at the subunit interface are charged at lower pH, forming salt bridges that stabilize the T state.
An increased affinity for O2 in the remaining subunits (which have not yet bound O2)
It covalently bonds heme into the hemoglobin subunit.
The T state is less stable than the R state at lower pH
As pH decreases, the O2 binding curve of hemoglobin shifts to the right, because a greater proportion of hemoglobin molecules exist in the T-state at a given pO2.
invariant residue
A heme prosthetic group is tightly bound to myoglobin via a coordination bond.
Oxygen is a homoallosteric effector of myoglobin.
The T state is less stable than the R state at lower pH.