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Protein Folding definitions

컨트롤 버튼이 '내비게이션' 모드로 변경되었습니다.
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  • Primary Structure
    Linear sequence of amino acids in a polypeptide chain, determining folding information through unique R groups.
  • Peptide Bond
    Covalent linkage connecting amino acids in a polypeptide, forming the backbone of protein structure.
  • Secondary Structure
    Local folding patterns of the polypeptide backbone, mainly alpha helices and beta sheets stabilized by hydrogen bonds.
  • Alpha Helix
    Rigid, cylindrical structure formed by hydrogen bonds between every fourth amino acid, common in skin proteins.
  • Beta Sheet
    Sheet-like arrangement of polypeptide segments, stabilized by hydrogen bonds, can be parallel or antiparallel.
  • Tertiary Structure
    Three-dimensional conformation of a single polypeptide, integrating motifs and domains for function and stability.
  • Structural Motif
    Combination of secondary structures forming a stable 3D unit, often with a specific function within a protein.
  • Coiled Coil
    Motif where two or three alpha helices wrap around each other, creating a stable, functional structure.
  • Protein Domain
    Independent, stable segment of a polypeptide, often recurring in different proteins and responsible for specific functions.
  • Domain Shuffling
    Evolutionary process mixing domains among proteins, generating new combinations and functional diversity.
  • Quaternary Structure
    Assembly of multiple polypeptide subunits, forming a functional protein complex with non-covalent or disulfide bonds.
  • Subunit
    Individual polypeptide chain within a multimeric protein, which may be identical or different from others.
  • Homodimer
    Protein complex composed of two identical polypeptide subunits.
  • Heterodimer
    Protein complex composed of two non-identical polypeptide subunits.
  • Unstructured Region
    Flexible, disordered segment of a protein, often providing adaptability and unique functional roles.