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Proteins definitions

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  • Amino Acids
    Building blocks of proteins, consisting of a central carbon, amino group, carboxyl group, and a variable R group.
  • Peptide Bonds
    Covalent bonds linking amino acids in a protein chain, forming between the amino group of one and the carboxyl group of another.
  • N-terminal
    The end of a protein or polypeptide chain with a free amino group.
  • C-terminal
    The end of a protein or polypeptide chain with a free carboxyl group.
  • Oligopeptides
    Short chains of amino acids, typically containing 2 to 20 residues.
  • Polypeptides
    Long chains of amino acids, generally containing more than 50 residues.
  • Primary Structure
    The sequence of amino acids in a protein, determining its unique characteristics.
  • Secondary Structure
    Local folding of a protein into alpha helices or beta sheets.
  • Tertiary Structure
    The overall 3D shape of a single polypeptide chain.
  • Quaternary Structure
    The arrangement of multiple polypeptide chains in a functional protein.
  • Denatured Proteins
    Proteins that have lost their functional shape due to environmental changes.
  • Chaperone Proteins
    Proteins that assist in the proper folding of other proteins.
  • Alpha Helices
    A common secondary structure in proteins, characterized by a coiled shape.
  • Beta Sheets
    A secondary structure in proteins, characterized by a zigzag pattern.
  • R Group
    The variable side chain of an amino acid that determines its properties.