Interactions of membranes with coarse-grain proteins : a comparison

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NEDER, Jörg, Peter NIELABA, Beate WEST, Friederike SCHMID, 2012. Interactions of membranes with coarse-grain proteins : a comparison. In: New Journal of Physics. 14(12), 125017. ISSN 1367-2630. eISSN 1367-2630. Available under: doi: 10.1088/1367-2630/14/12/125017

@article{Neder2012Inter-21137, title={Interactions of membranes with coarse-grain proteins : a comparison}, year={2012}, doi={10.1088/1367-2630/14/12/125017}, number={12}, volume={14}, issn={1367-2630}, journal={New Journal of Physics}, author={Neder, Jörg and Nielaba, Peter and West, Beate and Schmid, Friederike}, note={Article Number: 125017} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:contributor>Schmid, Friederike</dc:contributor> <dspace:hasBitstream rdf:resource=""/> <dcterms:title>Interactions of membranes with coarse-grain proteins : a comparison</dcterms:title> <dcterms:rights rdf:resource=""/> <dc:creator>West, Beate</dc:creator> <dc:contributor>West, Beate</dc:contributor> <dc:creator>Nielaba, Peter</dc:creator> <dcterms:isPartOf rdf:resource=""/> <bibo:uri rdf:resource=""/> <dc:date rdf:datatype="">2013-01-10T06:50:46Z</dc:date> <dcterms:hasPart rdf:resource=""/> <dc:contributor>Nielaba, Peter</dc:contributor> <dcterms:bibliographicCitation>New Journal of Physics ; 14 (2012), 12. - 125017</dcterms:bibliographicCitation> <dcterms:abstract xml:lang="eng">We study the interactions between lipid bilayers and rigid transmembrane proteins by Monte Carlo simulations of generic coarse-grain models. Different popular protein models are considered and compared with each other, and key parameters such as the hydrophobicity and the hydrophobic mismatch are varied systematically. Furthermore, the properties of the membrane are manipulated by applying different tensions. The response of the membrane to the insertion of single proteins is found to be mostly generic and independent of the choice of the protein model. Likewise, the orientational distributions of single proteins depend mainly on the hydrophobic mismatch and the hydrophobicity of the proteins, and are otherwise similar for all protein models. Orientational distributions are generally found to be very broad, i.e. tilt angles fluctuate very much, in agreement with experimental findings. Weakly hydrophobic proteins respond to positive hydrophobic mismatch by tilting. Strongly hydrophobic (strongly bound) proteins distort the surrounding membrane and tend to remain upright. For proteins with intermediate hydrophobicity, the two mechanisms compete, and as a result, the tilt only sets in if the hydrophobic mismatch exceeds a threshold. Clusters of several strongly hydrophobic proteins with negative positive mismatch may nucleate raft-like structures in membranes. This effect is more pronounced for proteins with rough, structured surfaces.</dcterms:abstract> <dcterms:issued>2012</dcterms:issued> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dspace:isPartOfCollection rdf:resource=""/> <dc:creator>Neder, Jörg</dc:creator> <dc:contributor>Neder, Jörg</dc:contributor> <dc:language>eng</dc:language> <dcterms:available rdf:datatype="">2013-01-10T06:50:46Z</dcterms:available> <dc:creator>Schmid, Friederike</dc:creator> <dc:rights>terms-of-use</dc:rights> </rdf:Description> </rdf:RDF>

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