TY  - JOUR
AU  - Khoshnood, A.
AU  - Noguchi, H.
AU  - Gompper, G.
TI  - Lipid membranes with transmembrane proteins in shear flow
JO  - The journal of chemical physics
VL  - 132
SN  - 0021-9606
CY  - Melville, NY
PB  - American Institute of Physics
M1  - PreJuSER-8000
SP  - 025101
PY  - 2010
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Computer Simulation
KW  - Friction
KW  - Membrane Lipids: chemistry
KW  - Membrane Proteins: chemistry
KW  - Models, Molecular
KW  - Membrane Lipids (NLM Chemicals)
KW  - Membrane Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:20095714
UR  - <Go to ISI:>//WOS:000273689000060
DO  - DOI:10.1063/1.3285269
UR  - https://juser.fz-juelich.de/record/8000
ER  -