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Proteins definitions

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  • Protein
    A functional biomolecule composed of one or more folded polypeptide chains, essential for cellular structure and function.
  • Amino Acid
    A monomeric unit with a central alpha carbon, amino group, carboxyl group, hydrogen, and a variable R group.
  • Peptide Bond
    A covalent linkage joining adjacent amino acids in a chain, forming the backbone of protein polymers.
  • N-terminal
    The end of a protein or polypeptide chain featuring a free amino group, marking the start of the sequence.
  • C-terminal
    The end of a protein or polypeptide chain with a free carboxyl group, indicating the chain's conclusion.
  • R Group
    A variable side chain attached to the alpha carbon of an amino acid, determining its unique properties.
  • Oligopeptide
    A short chain consisting of 2 to 20 covalently linked amino acids.
  • Polypeptide
    A linear chain of more than 50 amino acids, not necessarily in a functional folded state.
  • Primary Structure
    The specific sequence, type, and quantity of amino acids in a protein chain, dictating higher-level structures.
  • Secondary Structure
    Local folding patterns in a protein backbone, such as alpha helices and beta sheets, stabilized by hydrogen bonds.
  • Tertiary Structure
    The overall three-dimensional shape of a single polypeptide chain, resulting from interactions among side chains.
  • Quaternary Structure
    The association of multiple polypeptide chains to form a single functional protein complex.
  • Denatured Protein
    A nonfunctional form resulting from loss of native structure due to environmental changes like pH or temperature.
  • Chaperone Protein
    A helper molecule that assists other proteins in regaining or maintaining their correct folded structure.