It forms the outer layer of a cell. It gives an animal cell its shape. It is selectively permeable.
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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
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Answer:
Due to being nearsighted.
Explanation:
Nearsightedness can also be caused by the cornea and/or lens being too curved for the length of the eyeball. In some cases, myopia occurs due to a combination of these factor
the believe they move inside the membrane which is creating a gradient
On the off chance that there is an EcoR1 site in either the center of the Glo quality, or amidst the selectable marker site in the plasmid, it would likely debilitate either Glo, or the plasmid.I hope this will help.
