Difference Between Polar and Nonpolar Amino Acids
Characteristics |
Polar Amino Acids |
Non-Polar Amino Acids |
| Charge | Can be positively charged, negatively charged, or neutral | Neutral in charge |
| Hydrogen Bonding | Can form hydrogen bonds with polar molecules, including water and other polar amino acids | Cannot form hydrogen bonds with polar molecules |
| Solubility | Generally soluble in water | Generally insoluble in water |
| Location in Proteins | Often found on the surface of proteins | Often buried in the interior of proteins |
| Reactivity | More reactive due to their hydrophilic nature | Less reactive due to their hydrophobic nature |
| Specific examples | Serine, threonine, asparagine, lysine, arginine, glutamine, aspartic acid | Alanine, valine, leucine, isoleucine, phenylalanine, tryptophan, methionine |
| Function in proteins | Often involved in protein-protein interactions, enzymatic reactions, and ligand binding | Often involved in maintaining the stability of protein structures |
Difference Between Polar and Nonpolar Amino Acids
Polar and Non-Polar are two types of Amino Acids. Amino acids are organic compounds that are the building blocks of proteins. They contain both an amino group (-NH2) and a carboxyl group (-COOH) attached to the same carbon atom, known as the alpha carbon. The remaining side chain or R-group is what distinguishes one amino acid from another and determines its specific properties and functions.