Denaturation disrupts hydrogen bonds, leading to the unfolding of globules and uncoiling of helices. This process destroys secondary and tertiary structures while preserving the primary structure of proteins.

A native protein is a protein in a biological system with a unique three-dimensional structure and biological activity. Denaturation occurs when subjected to physical or chemical changes, disrupting hydrogen bonds, unfolding globules, and uncoiling helices, resulting in the loss of ...

Hydrogen bonds, disulphide linkages, van der Waals, and electrostatic forces stabilize the tertiary structure, representing the overall folding of polypeptide chains. The quaternary structure involves the spatial arrangement of subunits in proteins composed of two or more polypeptide chains.

Fat-soluble vitamins (A, D, E, K) are insoluble in water, stored in liver and adipose tissues, while water-soluble vitamins (B group, C) must be regularly supplied in the diet due to easy excretion except for vitamin B₁₂.

Coined from “vital” + “amine,” the term “vitamin” originally suggested compounds with amino groups. However, since most vitamins lack amino groups, the letter ‘e’ was dropped, and the term is used to describe essential organic compounds for health and growth.

Vitamins are organic compounds required in small amounts for specific biological functions, and their deficiency can lead to diseases. While most vitamins cannot be synthesized in our body, plants and gut bacteria contribute to our vitamin intake.

Enzymes, like chemical catalysts, lower activation energy for reactions. For instance, while acid hydrolysis of sucrose has an activation energy of 6.22 kJ mol⁻¹, sucrase, an enzyme, reduces it to 2.15 kJ mol⁻¹, demonstrating the efficiency of enzyme action.

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).