A spacefilled model of human insulin, Chain A is modeled in green and Chain B in blue.
A backbone model of human insulin
Disulfide bridges(yellow) and hydrogen bonds (red) stabilize the two human insulin chains.
This spacefilled model highlights human insulin's hydrophobic core (as shown in yellow). The white, hydrophilic outer amino acids interact directly with water.
This spacefilled model shows the concentration of certain carbon heavy amino acids(yellow) indicating the hydrophobic core and cysteine(green) which forms disulfide bonds, while many hydrophilic(white), positively(blue), and negative(red) are on the outer shell of insulin.
Human insulins largest difference from pig insulin is the presence of threonine(light blue) instead of alanine.
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Porcine Monomeric Insulin
(based on 4INS.pdb)
A spacefilled model of pig insulin. Chains A(green)and B(blue)that become bonded like human insulin
The backbone model of pig insulin looks identical to human insulin
Disulfide bridges(yellow) and hydrogen bonds (red) stabilize the two insulin chains.
This spacefilled model highlights pig insulins hydrophobic core (as shown in yellow). The white, hydrophilic outer amino acids interact directly with water.
This spacefilled model of shows the concentration of certain carbon heavy amino acids(yellow) indicating the hydrophobic core and cysteine(green) which forms disulfide bonds, while many hydrophilic(white), positively(blue), and negative(red) are on the outer shell of insulin.
The only difference between pig insulin and human insulin is the presence of an alanine amino acid(pink) instead of a threonine amino acid.
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References:
https://pdb101.rcsb.org/motm/14
https://www.rcsb.org/structure/2hiu