BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Nearly all globular proteins contain substantial numbers of -helices and -sheets folded into a compact structure that is stabilized by both polar and nonpolar interactions (Fig.

Detailed explanation-2: -Globular Protein Structure The secondary structure is the hydrogen bonding patterns that occur between amino acids in the polypeptide chain. There are two main structures that occur, alpha helices or beta-pleated sheets. A single polypeptide chain usually has some of both.

Detailed explanation-3: -Secondary structure is generated by formation of hydrogen bonds between atoms in the polypeptide backbone, which folds the chains into either alpha helices or beta-sheets. Tertiary structure is formed by the folding of the secondary structure sheets or helices into one another.

Detailed explanation-4: -Two folds that are extremely common in biochemistry are the alpha-helix and the beta-pleated sheet. The alpha-helix is a right-handed helical coil that is held together by hydrogen bonding between every fourth amino acid.

Detailed explanation-5: -There are three common secondary structures in proteins, namely alpha helices, beta sheets, and turns.