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Biochemistry Task 2
Paul A. Lebeck
000490213
January 26, 2016

A.

B.

(Borges, 2014, Wolfe, 2015).
C.

(Wolfe, 2015).
D.

(Wolfe, 2015).
E.
The forces, bonds, and interactions by protein structures at the Tertiary level.
There are Hydrophobic (nonpolar), Ionic bonds, Hydrogen (covalent) bonds, and
Disulfide bonds, also called Disulfide Bridges.
Hydrophobic are nonpolar bonds, meaning they cannot interact with water or aqueous solutions. Hydrophobic interactions will cause the protein to change shape to avoid making contact with such solutions. Considered weak bonds, but the proteins cluster tightly together on the interior of the protein, Van der Waals interaction take place between the proteins, again these are the weakest of the molecular bonds.
Ionic Bonds are by definition bonds that are made up of charged particles. There are 20 Amino Acids, some with negatively charged terminals, some with positively

charged terminals. This is a basic chemistry property that opposites attract.
These are considered stronger bonds, but not the strongest.
Next are hydrogen bonds. Considered stronger bonds than hydrophobic bonds, but weak compared to ionic and disulfide bonds. Hydrogen bonds are formed from Polar Covalent interactions. Two amino acids share a hydrogen electron and connect on the second amino acid oxygen atom. There must be a hydrogen donor on one amino acid, and a hydrogen acceptor on a second amino acid to complete the bond.
The strongest bond in the Tertiary level a disulfide bond. These occur only between two cysteine amino acids. There is a strong covalent bond when two cysteines are brought close together and they interact to form a bridge called a disulfide bond, or disulfide bridge. They are strong enough to hold two amino acid chains together or they can hold two side chains.
(Borges, 2014, Wolfe 2015).
F.

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