Suppose a hypothetical "molecule X" binds to hemoglobin (at a different site than the O2 binding site) and stabilizes the T state. How would you identify this effector? a. Positive homotropic effector b. Negative homotropic effector c. Positive heterotropic effector d. Negative heterotropic effector
Suppose a hypothetical "molecule X" binds to hemoglobin (at a different site than the O2 binding site) and stabilizes the T state. How would you identify this effector?
Hemoglobin is a globular protein, ie it is roughly spherical. It is a tetramer of two types of protein: α chain and β chain (this has nothing to do with alpha helix or beta sheets, the two polypeptide chains are labelled α and β). The α and β chains interact with one another to form a dimer (α1 β1) that interacts with another dimer (α2 β2) to form the tetramer.
There are two conformations in which hemoglobin can exist: R state and T state. R state has a higher affinity for oxygen. When oxygen is absent, hemoglobin exists in the T state. When oxygen binds to hemoglobin in the T state, it induces a change in conformation, from the T state to the R state.
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