In hemoglobin, the transition from t state to r state (low to high affinity) is triggered by Bisphosphoglycerate (BPG)
- Bisphosphoglycerate (BPG), also known as 2,3-Disphosphoglycerate (2,3-DPG), aids in the transition of hemoglobin from a high-oxygen-affinity to a low-oxygen-affinity state.
- 2,3-BPG binds to hemoglobin, causing oxygen to be unloaded. Furthermore, 2,3-BPG reduces hemoglobin's affinity for oxygen. As hemoglobin is unloaded in our tissues, 2,3-BPG binds to it, promoting oxygen unloading.
- When we increase the concentration of 2,3-BPG in our blood, the oxygen binding curve shifts to the right. This means hemoglobin will have a lower affinity for oxygen and will be able to deliver more oxygen to our body's tissues and cells.
Learn more about Bisphosphoglycerate (BPG) from here:brainly.com/question/8885734
#SPJ4
Answer:
Some of these proteins serve to transport materials into or out of the cell. Carbohydrates are attached to some of the proteins and lipids on the outward-facing surface of the membrane. These form complexes that function to identify the cell to other cells.
We eat and drink to obtain the energy and matter we use to survive
<span>a wading shorebird, such as a heron</span>
