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Tertiary Structure of Protein definitions

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  • Tertiary Structure
    Overall three-dimensional shape of a protein formed by folding and stabilized by interactions among R groups.
  • R Group
    Side chain of an amino acid responsible for unique chemical properties and interactions in protein structure.
  • Peptide Backbone
    Linear chain of amino acids in a protein, connecting N-terminal and C-terminal ends, supporting folding.
  • Ionic Bond
    Electrostatic attraction between ionizable side chains, often called salt bridges, stabilizing protein structure.
  • Salt Bridge
    Specific ionic interaction between oppositely charged amino acid side chains, contributing to protein stability.
  • Hydrophobic Effect
    Tendency of non-polar amino acid side chains to cluster together, driving protein folding and stability.
  • Hydrogen Bond
    Attraction between polar side chains, such as serine and asparagine, enhancing protein structural integrity.
  • Van der Waals Interaction
    Weak, non-covalent forces occurring between all atoms in a protein, providing general stabilization.
  • Disulfide Bridge
    Covalent bond formed between two cysteine residues, significantly reinforcing protein tertiary structure.
  • Cysteine
    Amino acid with a thiol side chain capable of forming disulfide bonds, crucial for protein stability.
  • Alpha Helix
    Spiral secondary structure segment within proteins, contributing to overall folding and tertiary shape.
  • Beta Sheet
    Extended secondary structure formed by aligned strands, influencing protein's three-dimensional arrangement.
  • Beta Turn
    Short segment causing abrupt change in backbone direction, connecting secondary structure elements.
  • Polypeptide Chain
    Sequence of amino acids linked by peptide bonds, capable of folding into complex protein structures.
  • Amino Acid
    Building block of proteins, each with a unique side chain that determines its role in structure and function.