zaro

What are the examples of amino acids in biochemistry?

Published in Amino Acids 2 mins read

Amino acids are the building blocks of proteins and play crucial roles in countless biochemical processes. Here are some examples of amino acids, categorized for clarity:

Acidic (Negatively Charged) Amino Acids

These amino acids have a net negative charge at physiological pH.

  • Aspartic Acid (Aspartate): Involved in the urea cycle and neurotransmission.
  • Glutamic Acid (Glutamate): The most abundant excitatory neurotransmitter in the vertebrate nervous system; also involved in metabolic pathways.

Basic (Positively Charged) Amino Acids

These amino acids have a net positive charge at physiological pH.

  • Lysine: Essential amino acid; important for protein synthesis and modification.
  • Arginine: Involved in the urea cycle; precursor to nitric oxide.
  • Histidine: Can be positively charged or neutral at physiological pH, often found in enzyme active sites due to its ability to act as both a proton donor and acceptor.

Nonpolar (Hydrophobic) Amino Acids

These amino acids tend to cluster together within proteins, away from water.

  • Alanine: Simple amino acid commonly found in proteins.
  • Valine: Branched-chain amino acid; essential for humans.
  • Leucine: Branched-chain amino acid; essential for humans.
  • Isoleucine: Branched-chain amino acid; essential for humans.
  • Methionine: Contains sulfur; important for initiation of translation and as a methyl group donor.
  • Phenylalanine: Aromatic amino acid; precursor to tyrosine.
  • Tryptophan: Aromatic amino acid; precursor to serotonin and melatonin.
  • Proline: Unique cyclic structure; often found in turns of protein structure.
  • Glycine: The smallest amino acid; often found in flexible regions of proteins.

Polar (Uncharged) Amino Acids

These amino acids have polar side chains but are not charged at physiological pH.

  • Serine: Contains a hydroxyl group; site for phosphorylation.
  • Threonine: Contains a hydroxyl group; site for phosphorylation and glycosylation.
  • Cysteine: Contains a thiol group; can form disulfide bonds.
  • Tyrosine: Aromatic amino acid; can be phosphorylated.
  • Asparagine: Amide derivative of aspartic acid.
  • Glutamine: Amide derivative of glutamic acid.

These examples represent a diverse group of amino acids, each with unique chemical properties that contribute to the structure and function of proteins. Understanding these properties is essential for comprehending biochemical processes.