Answer:
on a tyrosine residue
bind to insulin
Explanation:
The insulin receptor substrate-1 (IRS1) is a signaling protein that can be phosphorylated on multiple tyrosine and serine/threonine residues. IRS1 contains several conserved domains including a pleckstrin (PH) domain and a PTB domain involved in protein phosphorylation and ligand binding. In the first place, IRS1 is phosphorylated on a tyrosine residue, and then IRS1 binds to insulin or the insulin-like growth factor-1 (IGF-1), thereby activating transduction pathways such as, for example, MAPK/ERK. Moreover, RS1 is also phosphorylated on serine residues, thereby triggering opposite effects in insulin-associated signaling.
Enzymes are highly specific proteins that function best at certain pHs. A change in pH would affect its structure; too high or too low would cause denaturation. When this happens, the enzyme won’t have the correct structure to function as a catalyst. Therefore, reaction rate will slow.
Hope this helps!!
Answer: radiation i think
Answer:
1. Water will move out of the cell
- There is a higher concentration outside of the cell
Answer:
the answer for is heterozygous
