Random pinning limits the size of membrane adhesion domains
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Thomas Speck
- Richard LC Vink
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000309338900005&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1103/PhysRevE.86.031923
- eISSN
- 1550-2376
- Externe Identifier
- Clarivate Analytics Document Solution ID: 013XH
- PubMed Identifier: 23030960
- ISSN
- 1539-3755
- Ausgabe der Veröffentlichung
- 3
- Zeitschrift
- PHYSICAL REVIEW E
- Artikelnummer
- ARTN 031923
- Datum der Veröffentlichung
- 2012
- Status
- Published
- Titel
- Random pinning limits the size of membrane adhesion domains
- Sub types
- Article
- Ausgabe der Zeitschrift
- 86
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Thomas Speck
- Richard LC Vink
- DOI
- 10.1103/physreve.86.031923
- eISSN
- 1550-2376
- ISSN
- 1539-3755
- Ausgabe der Veröffentlichung
- 3
- Zeitschrift
- Physical Review E
- Sprache
- en
- Artikelnummer
- 031923
- Online publication date
- 2012
- Status
- Published online
- Herausgeber
- American Physical Society (APS)
- Herausgeber URL
- http://dx.doi.org/10.1103/physreve.86.031923
- Datum der Datenerfassung
- 2017
- Titel
- Random pinning limits the size of membrane adhesion domains
- Ausgabe der Zeitschrift
- 86
Datenquelle: Crossref
- Abstract
- Theoretical models describing specific adhesion of membranes predict (for certain parameters) a macroscopic phase separation of bonds into adhesion domains. We show that this behavior is fundamentally altered if the membrane is pinned randomly due to, e.g., proteins that anchor the membrane to the cytoskeleton. Perturbations which locally restrict membrane height fluctuations induce quenched disorder of the random-field type. This rigorously prevents the formation of macroscopic adhesion domains following the Imry-Ma argument [Imry and Ma, Phys. Rev. Lett. 35, 1399 (1975)]. Our prediction of random-field disorder follows from analytical calculations and is strikingly confirmed in large-scale Monte Carlo simulations. These simulations are based on an efficient composite Monte Carlo move, whereby membrane height and bond degrees of freedom are updated simultaneously in a single move. The application of this move should prove rewarding for other systems also.
- Addresses
- Institut für Theoretische Physik II: Weiche Materie, Heinrich-Heine-Universität Düsseldorf, Universitätsstrasse 1, D-40225 Düsseldorf, Germany.
- Autoren
- Thomas Speck
- Richard LC Vink
- DOI
- 10.1103/physreve.86.031923
- eISSN
- 1550-2376
- Externe Identifier
- PubMed Identifier: 23030960
- Open access
- false
- ISSN
- 1539-3755
- Ausgabe der Veröffentlichung
- 3 Pt 1
- Zeitschrift
- Physical review. E, Statistical, nonlinear, and soft matter physics
- Schlüsselwörter
- Cell Membrane
- Monte Carlo Method
- Stochastic Processes
- Cell Adhesion
- Models, Biological
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2012
- Paginierung
- 031923
- Datum der Veröffentlichung
- 2012
- Status
- Published
- Datum der Datenerfassung
- 2012
- Titel
- Random pinning limits the size of membrane adhesion domains.
- Sub types
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 86
Datenquelle: Europe PubMed Central
- Abstract
- Theoretical models describing specific adhesion of membranes predict (for certain parameters) a macroscopic phase separation of bonds into adhesion domains. We show that this behavior is fundamentally altered if the membrane is pinned randomly due to, e.g., proteins that anchor the membrane to the cytoskeleton. Perturbations which locally restrict membrane height fluctuations induce quenched disorder of the random-field type. This rigorously prevents the formation of macroscopic adhesion domains following the Imry-Ma argument [Imry and Ma, Phys. Rev. Lett. 35, 1399 (1975)]. Our prediction of random-field disorder follows from analytical calculations and is strikingly confirmed in large-scale Monte Carlo simulations. These simulations are based on an efficient composite Monte Carlo move, whereby membrane height and bond degrees of freedom are updated simultaneously in a single move. The application of this move should prove rewarding for other systems also.
- Autoren
- Thomas Speck
- Richard LC Vink
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/23030960
- DOI
- 10.1103/PhysRevE.86.031923
- eISSN
- 1550-2376
- Ausgabe der Veröffentlichung
- 3 Pt 1
- Zeitschrift
- Phys Rev E Stat Nonlin Soft Matter Phys
- Schlüsselwörter
- Cell Adhesion
- Cell Membrane
- Models, Biological
- Monte Carlo Method
- Stochastic Processes
- Sprache
- eng
- Country
- United States
- Paginierung
- 031923
- Datum der Veröffentlichung
- 2012
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2013
- Titel
- Random pinning limits the size of membrane adhesion domains.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 86
Datenquelle: PubMed
- Abstract
- Theoretical models describing specific adhesion of membranes predict (for certain parameters) a macroscopic phase separation of bonds into adhesion domains. We show that this behavior is fundamentally altered if the membrane is pinned randomly due to, e.g., proteins that anchor the membrane to the cytoskeleton. Perturbations which locally restrict membrane height fluctuations induce quenched disorder of the random-field type. This rigorously prevents the formation of macroscopic adhesion domains following the Imry-Ma argument [Y. Imry and S. K. Ma, Phys. Rev. Lett. 35, 1399 (1975)]. Our prediction of random-field disorder follows from analytical calculations, and is strikingly confirmed in large-scale Monte Carlo simulations. These simulations are based on an efficient composite Monte Carlo move, whereby membrane height and bond degrees of freedom are updated simultaneously in a single move. The application of this move should prove rewarding for other systems also.
- Autoren
- Thomas Speck
- Richard LC Vink
- Autoren-URL
- http://arxiv.org/abs/1203.2493v2
- Zeitschrift
- Phys. Rev. E
- Schlüsselwörter
- cond-mat.stat-mech
- cond-mat.stat-mech
- cond-mat.soft
- physics.bio-ph
- Notes
- revised and extended version
- Paginierung
- 031923
- Datum der Veröffentlichung
- 2012
- Herausgeber URL
- http://dx.doi.org/10.1103/PhysRevE.86.031923
- Datum der Datenerfassung
- 2012
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2012
- Titel
- Random pinning limits the size of membrane adhesion domains
- Ausgabe der Zeitschrift
- 86
Files
1203.2493v2.pdf
Datenquelle: arXiv
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