Skip to main content
Back

Proteins definitions

Control buttons has been changed to "navigation" mode.
1/15
  • Amino Acid
    Building block with a unique R group, amino group, and carboxyl group, determining protein properties and structure.
  • Polypeptide Chain
    Linear sequence of amino acids linked together, forming the backbone of protein structure.
  • Primary Structure
    Specific order of amino acids in a chain, dictating all higher levels of protein organization.
  • Secondary Structure
    Local folding patterns like alpha helices and beta sheets, stabilized by interactions between nearby residues.
  • Alpha Helix
    Spiral-shaped local structure within a protein, stabilized by hydrogen bonds between backbone atoms.
  • Beta Sheet
    Sheet-like arrangement formed by aligned polypeptide strands, which can be parallel or antiparallel.
  • Tertiary Structure
    Overall 3D shape of a single polypeptide chain, integrating multiple secondary structures.
  • Quaternary Structure
    Three-dimensional arrangement of multiple polypeptide chains, contributing to protein function.
  • N-terminus
    Start of a polypeptide chain, marked by a free amino group.
  • C-terminus
    End of a polypeptide chain, marked by a free carboxyl group.
  • R Group
    Variable side chain of an amino acid, responsible for its unique chemical properties.
  • Globular Protein
    Compact, roughly spherical protein shape, often associated with dynamic biological functions.
  • Fibrous Protein
    Elongated, linear protein shape, typically providing structural support.
  • Domain
    Distinct structural region within a protein, often associated with a specific function.
  • Chaperone
    Helper molecule ensuring correct protein folding, preventing misfolding or aggregation.