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30.04.2008Physik der Lipide
hydrophobe Wechselwirkung kritische MizellkonzentrationPermeabilitätDiffusion
Biophysik der Zelle
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Inhalt• The structure of the plasma membrane• Biochemistry of lipids• Hydrophobic effect, • Micelle formation• Packing Parameter and Tanford Modell• Transport across membranes• Diffusion in membranes
Literatur:„Structure and Dynamics of Membranes“, Sackmann, Lipowsky editors, Springer„Life-as a Matter of Fat“, O. Mouritsen, Springer 2005„Intermolecular & Surface Forces“, Israelachvili, Acad.Press, 2nd Ed. 2005Sackmann Skript: Kapitel Membranen
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Fluid-Mosaic Model
Nicholson& Singer 1977
Proteins diffuse freelyin a fluid matrix of lipid
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Lipid membranes ascomposite materials
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The structure of the spectrin network
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Lipide
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Due to the amphipathic nature of phospholipids,these molecules spontaneously assemble to formclosed bilayers
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Phospholipid structure
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Bilder Membranes
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Cholesterol
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Fettsäuren
218CH3(CH2)4CH=CHCH2CH=CH(CH2)7COOH
Linolsäure
118CH3(CH2)7CH=CH(CH2)7
-COOHOleinsäure
020CH3(CH2)18COOHArchinsäuren -Eicodekansäure
018CH3(CH2)16COOHStearinsäuren -Octadekansäure
016CH3(CH2)14COOHPalmitinsäuren -Hexadekansäure
014CH3(CH2)12COOHMyristinsäuren -Tetradekansäure
A n z a h l d e rungesättigtenBindungen
Anzahl derC-Atome
StrukturTrivialnameName
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Nomenclature
DMPC: Dimyristoyl-Phosphatidyl-Cholin
DPPC: Dipalmitoyl-Phosphatidyl-Cholin
DSPC: Distearoyl-Phosphatidyl-Cholin
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Amphiphile Moleküle assoziieren zu Aggregaten
Lipid-Monolagen
Seifenfilm
Mizelle
Lipid-Doppelschicht
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Solubility and partitition function
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The critical micelle concentration, where further addition of solute moleculesresult in the formation of more aggregates, while leaving the momomerconcentration constant.
Thermodynamics of lipid aggregation
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The hydrophobic effect
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Morphologien von Lipidaggregaten
Mizelle
Stäbchenmizelle
Vesikel
Invertierte Mizelle
Bilayer
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V: Volumea0: cross section of headgroupl: alcyl chain length
The Packing-Parameter
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The Tanford Modell of opposing forces
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Pulling a single lipid out of a membrane
Die Entbindungskraft ist für PC-C14:0 f*≈ 12 pN. Das entspricht einer Bindungsenergiepro Molekül von Δg*~5 kBT die ein Faktor 5 kleiner ist als nach dem hydrophobenEffekt erwartet.
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H. Grubmüller, Göttingen
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Forcefields
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Lipid bilayer consisting of 512 POPC lipids.
Grubmüller group, MPI Göttingen
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Efficient, robust and tunable solvent-free bilayer modelIra R. Cooke, Kurt Kremer, and Markus DesernoPHYSICAL REVIEW E 72, 011506 2005
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Outcome of physical parameters: Observables
• Diffusion constant• orientational order parameter• flip-flop rate• bending modulus• compressibility modulus• rupture tension
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TRANSPORT
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A pure phospholipid bilayer acts as a selectivelypermeable barrier
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Diffusive flux across a membrane
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Flux across an energy barrier
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Transepithelial movement of glucose and amino acidsrequires multiple transport proteins
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Six ways in which membrane proteins associate with the lipid bilayer. Most trans-membrane proteins arethought to extend across the bilayer as a single α helix (1) or as multiple α helices (2); some of these"single-pass" and "multipass" proteins have a covalently attached fatty acid chain inserted in the cytoplasmicmonolayer (1). Other membrane proteins are attached to the bilayer solely by a covalently attached lipid -either a fatty acid chain or prenyl group - in the cytoplasmic monolayer (3) or, less often, via anoligosaccharide, to a minor phospholipid, phosphatidylinositol, in the noncytoplasmic monolayer (4). Finally,many proteins are attached to the membrane only by noncovalent interactions with other membrane proteins(5) and (6).
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Overview of membrane transport proteins
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Muscle Ca2+ ATPase pumps Ca2+ ions from thecytosol into the sarcoplasmic reticulum
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Na+/K+ ATPase maintains the intracellular Na+ and K+
concentrations in animal cells
Sackmann script
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Proposed model for operation of the two-Na+/one-glucose symporter
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Aquaporin
http://www.mpibpc.gwdg.de/abteilungen/071/bgroot/gallery.html
Chemistry Nobel Prize 2003
Die Wasserleitfähigkeit eines Aquaporinkanals beträgt bis zu 3 Milliarden Moleküle pro Sekunde.
Peter Agre
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Aquaporin-1 in action. Simulation fragment of 200 ps of aquaporin-1. Generated using Molscript/Bobscript and raster3d.
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„Real time“ moleculardynamics simulation
Aquaglyceroporin tetramer (blue, cyan, orange, magenta), embedded within a POPElipid bilayer(yellow head groups and green tails) surrounded by water (red,white).The total system consists of about 101,000 atoms.
Overlaid snapshots from a trajectory of a water molecule passing through AQP1 (leftand middle panels, surface and ribbon representation of the same protein structure)and hydrogen bond energies per water molecule (right). The permeation eventshown on the left lasted 3.3 ns.
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Molecular Dynamics of lipid bilayers
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Random walks
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from
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Snap shots
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Mobility in the plasma membrane
Jacobson, et al. Science 268 (1995) 5216