What is the Difference Between Acidic and Basic Amino Acids?

The difference between acidic and basic amino acids lies in the nature of their side chains and how they react with hydrogen ions (protons). Here are the key differences:

1. Acidic Amino Acids: These amino acids have side chains containing carboxylic acid groups with pKa values low enough to lose a proton at neutral pH. At neutral pH, acidic amino acids have negatively charged side chains. Examples of acidic amino acids include aspartic acid (Asp) and glutamic acid (Glu).
2. Basic Amino Acids: These amino acids have side chains with an additional amino group and relatively high pKa values, which are high enough to bind protons at neutral pH. Basic amino acids are positively charged at neutral pH. Examples of basic amino acids include arginine, histidine, lysine, and threonine.

In summary:

• Acidic amino acids:
• pKa values of side chains

Comparative Table: Acidic vs Basic Amino Acids

The main difference between acidic and basic amino acids lies in the nature of their side chains and the charges they carry at neutral pH. Here is a table comparing the characteristics of acidic and basic amino acids:

Acidic amino acids have acidic side chains and carry a net negative charge at neutral pH, while basic amino acids have basic side chains and carry a net positive charge at neutral pH. The pKa values of acidic amino acids are low, indicating their acidic nature, while the pKa values of basic amino acids are high, indicating their basic nature. Both acidic and basic amino acids are polar and hydrophilic, meaning they are soluble in water and can interact with other polar molecules.