fluid mosaic model Oligosaccharide hains of glyco Outside Glycolipid bilayer chain Phospholipid o3.]9 polar heads Inside Sterol Peripberal protein Integral protein Peripheral protein ( single trans covalently linked Integral protein membrane helix) to lipid (multiple trans membrane helices
Fluid mosaic model
1.3.2 Release of integral proteins from membranes requires detergents to interfere the hydrophobic interactions between proteins and surrounding lipids. 1.3.3 Released integral proteins are usually water-insoluble(easily precipitate to form insoluble aggregates)when the detergents are removed. 1.3.4 Integral proteins usually have one or more domains rich in hydrophobic amino acid residues 1.3.5 Transmembrane domains of a protein can be predicted with reasonable accuracy through hydropathy plotting
1.3.2 Release of integral proteins from membranes requires detergents to interfere the hydrophobic interactions between proteins and surrounding lipids. 1.3.3 Released integral proteins are usually water-insoluble (easily precipitate to form insoluble aggregates) when the detergents are removed. 1.3.4 Integral proteins usually have one or more domains rich in hydrophobic amino acid residues. 1.3.5 Transmembrane domains of a protein can be predicted with reasonable accuracy through hydropathy plotting
03 50 100130 0 HY ydrophobic Hydrophilic 6>士 0 50 100130 R esidue number Glycophorin a
1050 100150200250 3 TTTT 3 4 Hydrophobic Hydrophilic 3 1050100150200250 Residue number Bacteriorhodopsin
1.3.6 The three-dimensional structure of the hotosvnthet tic read er of a pul bacterium was the first integral membrane protein to have its atomic structure determined y X-ray crystallography, where hydrophobic residues are on the exterior interacting with the lipid bilayer 1.3.7 Some proteins, called peripheral proteins, are bound to membranes loosely and reversibly
1.3.6 The three-dimensional structure of the photosynthetic reaction center of a purple bacterium was the first integral membrane protein to have its atomic structure determined by X-ray crystallography, where hydrophobic residues are on the exterior interacting with the lipid bilayer. 1.3.7 Some proteins, called peripheral proteins, are bound to membranes loosely and reversibly