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Integral Membrane Proteins definitions

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  • Integral Membrane Protein
    Membrane-embedded molecule tightly anchored within the lipid bilayer, often requiring detergents for isolation due to strong membrane association.
  • Lipid Bilayer
    Double-layered structure forming the membrane, providing a hydrophobic environment that stabilizes certain protein conformations.
  • Alpha Helix
    Spiral secondary structure frequently found in membrane-embedded proteins, stabilized by hydrophobic surroundings.
  • Transmembrane Spanning Domain
    Segment crossing the membrane, typically composed of an alpha helix, anchoring the protein within the bilayer.
  • Loop
    Flexible connector linking multiple transmembrane domains, often located at the membrane surface.
  • Porin
    Channel-forming protein with a beta barrel motif, facilitating passage of specific polar molecules across membranes.
  • Beta Barrel
    Cylindrical motif formed by anti-parallel beta sheets, creating a hydrophilic interior and hydrophobic exterior.
  • Anti-parallel Beta Sheet
    Secondary structure where adjacent strands run in opposite directions, contributing to beta barrel formation.
  • Hydrophobic Environment
    Non-polar region within the membrane, stabilizing certain protein structures and influencing folding patterns.
  • Hydrophilic Interior
    Water-attracting central region of a beta barrel, enabling selective passage of polar molecules.
  • Hydrophobic Exterior
    Outer surface of a beta barrel motif, interacting with the membrane's non-polar lipid environment.
  • Motif
    Distinct pattern or combination of secondary structures within a protein, such as the beta barrel.
  • Glycophorin
    Example of a membrane protein with a single alpha helix, illustrating a single transmembrane domain.
  • Rhodopsin
    Membrane protein with multiple alpha helices, demonstrating several transmembrane domains.
  • Endosymbiotic Theory
    Concept explaining the presence of porins in mitochondria and chloroplasts due to their bacterial ancestry.