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.
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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).
Enzymes act as biocatalysts facilitating specific reactions like digestion, absorption, and energy production in living organisms. They are crucial for life processes due to their ability to catalyze reactions under mild conditions.
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.