Hauptseite > Publikationsdatenbank > Lipid membranes with transmembrane proteins in shear flow > print |
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024 | 7 | _ | |a 10.1063/1.3285269 |2 DOI |
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037 | _ | _ | |a PreJuSER-8000 |
041 | _ | _ | |a eng |
082 | _ | _ | |a 540 |
084 | _ | _ | |2 WoS |a Physics, Atomic, Molecular & Chemical |
100 | 1 | _ | |a Khoshnood, A. |b 0 |u FZJ |0 P:(DE-Juel1)VDB89986 |
245 | _ | _ | |a Lipid membranes with transmembrane proteins in shear flow |
260 | _ | _ | |a Melville, NY |b American Institute of Physics |c 2010 |
300 | _ | _ | |a 025101 |
336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
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336 | 7 | _ | |a article |2 DRIVER |
440 | _ | 0 | |a Journal of Chemical Physics |x 0021-9606 |0 3145 |y 2 |v 132 |
500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
520 | _ | _ | |a The effects of embedded proteins on the dynamical properties of lipid bilayer membranes are studied in shear flow. Coarse-grained molecular simulations are employed, in which lipids are modeled as short polymers consisting of hydrophilic head groups and hydrophobic tail monomers; similarly, transmembrane proteins are modeled as connected hydrophobic double- or triple-chain molecules with hydrophilic groups at both ends. In thermal equilibrium, rigid proteinlike molecules aggregate in a membrane of flexible lipids, while flexible proteins do not aggregate. In shear flow parallel to the membrane, the monolayers of lipid bilayer slide over each other. The presence of transmembrane proteins enhances the intermonolayer friction. The friction coefficient depends on the chain lengths of lipids, the membrane tension, the length of the protein, and the cluster size. It is found to increase with protein length (with positive mismatch, i.e., proteins which are longer than the membrane thickness) and protein cluster size. In flow, proteins get oriented in the flow direction to reduce friction, with large fluctuations of the orientation angle. |
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588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
650 | _ | 2 | |2 MeSH |a Computer Simulation |
650 | _ | 2 | |2 MeSH |a Friction |
650 | _ | 2 | |2 MeSH |a Membrane Lipids: chemistry |
650 | _ | 2 | |2 MeSH |a Membrane Proteins: chemistry |
650 | _ | 2 | |2 MeSH |a Models, Molecular |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Membrane Lipids |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Membrane Proteins |
650 | _ | 7 | |a J |2 WoSType |
653 | 2 | 0 | |2 Author |a aggregation |
653 | 2 | 0 | |2 Author |a biological fluid dynamics |
653 | 2 | 0 | |2 Author |a biomechanics |
653 | 2 | 0 | |2 Author |a biomembranes |
653 | 2 | 0 | |2 Author |a cellular biophysics |
653 | 2 | 0 | |2 Author |a friction |
653 | 2 | 0 | |2 Author |a hydrophilicity |
653 | 2 | 0 | |2 Author |a hydrophobicity |
653 | 2 | 0 | |2 Author |a lipid bilayers |
653 | 2 | 0 | |2 Author |a molecular biophysics |
653 | 2 | 0 | |2 Author |a molecular dynamics method |
653 | 2 | 0 | |2 Author |a proteins |
653 | 2 | 0 | |2 Author |a shear flow |
700 | 1 | _ | |a Noguchi, H. |b 1 |u FZJ |0 P:(DE-Juel1)VDB37578 |
700 | 1 | _ | |a Gompper, G. |b 2 |u FZJ |0 P:(DE-Juel1)130665 |
773 | _ | _ | |a 10.1063/1.3285269 |g Vol. 132, p. 025101 |p 025101 |q 132<025101 |0 PERI:(DE-600)1473050-9 |t The @journal of chemical physics |v 132 |y 2010 |x 0021-9606 |
856 | 7 | _ | |u http://dx.doi.org/10.1063/1.3285269 |
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