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The order in which the amino-acids are placed within the polypeptide determines the tertiary structure and therefore the function of the given protein. Amino acids have different functional groups like methyl(CH3), phenyl(C6H5). Those functional groups can interact with molecules like glucose determining reactions, the proteins that catalyze reactions are called enzymes. Other functional groups of amino acids can be the sulfate groups. For example, insulin has 2 polypeptide chains(Chain A has 21 amino acids, and chain B, 30). Between the two polypeptide chains, 2 disulfide bonds form altering its shape.

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The  secondary structure of a protein is generated by hydrogen bonds between atoms of the polypeptide backbone.

  • A hydrogen bond is an intramolecular attraction between a hydrogen atom in one molecule and an electronegative atom (e.g., oxygen) of another molecule.

  • The most common types of secondary structures in proteins are alpha helices and beta sheets.

  • In alpha helices, the carbonyl group of one amino acid is bonded to the amino group of another amino acid spaced four residues apart in the polypeptide chain.

  • In beta-sheets, different regions of the polypeptide line up next to each other, thereby these protein regions interact by hydrogen bonds.

In conclusion, the secondary structure of a protein is generated by hydrogen bonds between atoms of the polypeptide backbone.

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