Small mol: BPG locks hemoglobin
BPG's primary feature is that it's a small molecule bearing two phosphate groups (PO42-), and thus a lot of negative charge. Initially, BPG rests in a welcoming pocket of the oxygen-releasing form of hemoglobin.
Let's take a closer look at the pocket where BPG sits (deoxy form) or can't get in (oxy form). Use these controls to explore:
Highlight the following amino acids to answer the questions in the exercises:
Use the different conformations and the two labeling formats to answer the questions in the exercises.
The following can be used to answer a separate question about fetal hemoglobin: One way a fetus manages to steal oxygen from its mother's blood indirectly involves BPG. Fetuses use a different beta-globin gene which has several changes from the adult form. One of these is a change in the amino acid called for at position 143. Unlike the histidine shown, fetal hemoglobin would have a serine. Click the checkbox below to highlight this position. amino acid changed in fetal hemoglobin