The two different molecules of aquaporin will have different sequences of amino acids
Explanation:
Aquaporins are an integral type of membrane proteins. They act as water channels and their function is to transport water and other solute materials across cells membranes and thereby control and regulate the water content of the cells.
They are formed by clustering of four water channel monomers forming a tetramer.
Each aquaporin is made up of a specific linear sequence of amino acids and variations in the sequence leads to formation of different aquaporins.
There are more than 10 types of aquaporins are known. The sizes of the aquaporins differ according to their pore diameter of each type and this difference leads to the selective permeability of water across cell membranes.
Answer:Enzymes that makes redox reactions possible in a biochemical process includes those that help to catalyze the transfer of electrons, atoms, or functional groups.
Explanation:
Here are some class categories of these enzymes and their roles ;
• Oxidoreductases - Transfer of electrons (hydride ions or H atoms)
• Transferases - Group- transfer reactions
• Hydrolases - Hydrolysis reactions (transfer of functional groups to water)
• Lyases - Addition of groups to double bonds, or formation of double bonds by removal of groups Transfer of groups within molecules to yield isomeric forms
• Isomerases - Formation of C-C, C-S, C--0, and C-N bonds by condensation reactions coupled to ATP cleavage
The above are however classified, given code numbers, and assigned names according to the type of transfer reaction, the group donor, and the group acceptor.
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:
c. birds are baited by the metal hook...
Explanation:
The initial source of energy is sunlight
