Enzymes are named based on the specific reaction they catalyze or the substrate they act upon. The -ase ending is common in enzyme names, indicating their nature as catalysts (e.g., maltase catalyzes maltose hydrolysis).

Proteins exhibit two secondary structures, a-helix, and b-pleated sheet, resulting from hydrogen bonding between >C=O and –NH– groups in the peptide bond. The a-helix forms a right-handed screw, while the b-pleated sheet resembles pleated folds of drapery.

The primary structure of proteins refers to the specific sequence of amino acids in a polypeptide chain. Any alteration in this sequence creates a distinct protein, making the primary structure crucial for protein identity.

Protein structure can be studied at four levels: primary, secondary, tertiary, and quaternary. Each level represents increasing complexity, with primary being the simplest and quaternary being the most complex.

Globular proteins have a spherical shape formed as polypeptide chains coil around. They are generally soluble in water. Examples of globular proteins include insulin and albumins.

Fibrous proteins have a fiber-like structure with parallel polypeptide chains held together by hydrogen and disulphide bonds. Examples include keratin (in hair, wool, silk) and myosin (in muscles).

A protein is a polypeptide with more than a hundred amino acid residues, having a molecular mass higher than 10,000u. However, the distinction is not sharp, and polypeptides with fewer amino acids might be called proteins if they exhibit a ...

Dipeptide is a product of the combination of two amino acids through a peptide bond. Similarly, tripeptide, tetrapeptide, and polypeptide are formed by the linkage of three, four, and more than ten amino acids, respectively, through peptide linkages.

A peptide bond, also known as a peptide linkage, is an amide formed between the -COOH group and -NH₂ group of amino acids. It is created through a reaction between the amino group of one amino acid and the carboxyl ...