Ms.Carlson

Ms.Carlson

1.

1) Primary a linear like structure containing covalent bonding linking two consecutive amino acid monomers along a protein chain. Amino acid is hold together by a peptide bond.

2) Secondary has two main types of structures, the helix and the B Pleated sheet. The secondary structure is hold by hydrogen bonds between the main chain peptide groups.

3) Tertiary is an irregular folds containing hydrogen bond, disulfide bond, and ionic bond.

4) Quaternary has two or more polypeptides. Bonding included the same like tertiary structure with hydrogen bond between polar group, and disulfide bond.

2.

a) Cysteine contains sulfhydryl R-group.

b) R-group interacts with protein structure by attaching itself to carbon. Also, known as the side chain it can interact with each other with weak bond such as, hydrogen bond, ionic bond, and van der Waals forces. Therefore, cause the polypeptide backbone to fold like the secondary structure, and tertiary structure.

c) R-group is mainly use on Secondary and Tertiary structures. R-group in Secondary structure helps bends, and twists the polypeptide into 3-d shape. Therefore, extend away from the backbone of the chain in the opposite direction for the B pleated sheet. In Tertiary structure there’s two types of R-groups. One is a hydrophilic, and likes to interact with water. It reinforces the bigger protein molecule and helps keep it in solution whereas, the hydrophobic R-group is inside the folding macromolecule away from water. Therefore, which hold the three dimensional shape.

3.

a. Insulin is a powerful anabolic hormone that increasing the synthesis of DNA, RNA, nucleic acids and proteins in target tissues. Insulin inhibits hepatic glycogenolysis and converts the liver into an organ of glucose uptake and fuel storage (Laron, Z. 2008).

b. The structure will lose its form such as the three dimensional shape. Because, the sulfhydryl group contain the (-S-H) side group which contain...