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Protein Motifs and Domains definitions

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  • Tertiary Structure
    Three-dimensional arrangement formed by the combination of secondary structures, resulting in the overall shape of a protein.
  • Secondary Structure
    Local folding patterns within a polypeptide, including alpha helices, beta strands, beta turns, and loops.
  • Alpha Helix
    Spiral-shaped secondary structure stabilized by hydrogen bonds, often found in motifs and domains.
  • Beta Strand
    Extended, zigzag secondary structure that can pair with others to form beta sheets or motifs.
  • Beta Turn
    Short segment causing a reversal in polypeptide direction, often connecting secondary structures.
  • Loop
    Flexible, non-repetitive region connecting elements of secondary structure, often part of motifs.
  • Motif
    Specific pattern of secondary structures forming super secondary structures with distinct functions.
  • Helix-Loop-Helix
    Motif consisting of two alpha helices separated by a loop, commonly involved in binding.
  • Coiled Coil
    Motif where two alpha helices wind around each other, providing structural strength.
  • Beta-Alpha-Beta
    Motif featuring a beta strand, an alpha helix, and another beta strand in sequence.
  • Hairpin Motif
    Motif with two antiparallel beta strands connected by a small loop, forming a tight turn.
  • Domain
    Independently folding unit within a polypeptide, composed of motifs and capable of separate function.
  • Polypeptide Chain
    Linear sequence of amino acids forming the backbone of protein structure, containing domains and motifs.
  • Subunit
    Distinct polypeptide chain in a multi-chain protein, not connected to the backbone of other chains.
  • Peptide Backbone
    Continuous chain of amino acids forming the structural framework of a protein.