Close-up view of the modifications of fluid membranes due to phospholipase A2

Research output: Contribution to journalJournal articlepeer-review

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Close-up view of the modifications of fluid membranes due to phospholipase A2. / Jakobsen, Ask F.; Mouritsen, Ole G.; Weiss, Matthias.

In: Journal of Physics Condensed Matter, Vol. 17, No. 47, 30.11.2005, p. S4015-S4024.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Jakobsen, AF, Mouritsen, OG & Weiss, M 2005, 'Close-up view of the modifications of fluid membranes due to phospholipase A2', Journal of Physics Condensed Matter, vol. 17, no. 47, pp. S4015-S4024. https://doi.org/10.1088/0953-8984/17/47/025

APA

Jakobsen, A. F., Mouritsen, O. G., & Weiss, M. (2005). Close-up view of the modifications of fluid membranes due to phospholipase A2. Journal of Physics Condensed Matter, 17(47), S4015-S4024. https://doi.org/10.1088/0953-8984/17/47/025

Vancouver

Jakobsen AF, Mouritsen OG, Weiss M. Close-up view of the modifications of fluid membranes due to phospholipase A2. Journal of Physics Condensed Matter. 2005 Nov 30;17(47):S4015-S4024. https://doi.org/10.1088/0953-8984/17/47/025

Author

Jakobsen, Ask F. ; Mouritsen, Ole G. ; Weiss, Matthias. / Close-up view of the modifications of fluid membranes due to phospholipase A2. In: Journal of Physics Condensed Matter. 2005 ; Vol. 17, No. 47. pp. S4015-S4024.

Bibtex

@article{5a32967520fc4220b0188fdbb7a8cc0a,
title = "Close-up view of the modifications of fluid membranes due to phospholipase A2",
abstract = "Phospholipases are a class of molecular machines that are involved in the active remodelling processes of biological membranes. These lipases are interfacially activated enzymes and in the specific case of phospholipase A 2 (PLA2) the enzyme catalyses the hydrolysis of di-acyl phospholipids into products of lysolipids and fatty acids, that dramatically change the physical properties of lipid membrane substrates. Using dissipative particle dynamics simulations on a simple coarse-grained bead-spring model of a fluid lipid bilayer in water, the mechanical and diffusive properties of the bilayer in the pure state and after the action of PLA2 have been calculated. It is found that, in response to hydrolysis, the lipid membrane becomes mechanically softened and the various in-plane and trans-bilayer diffusional modes become enhanced. The results compare favourably with available experimental data.",
author = "Jakobsen, {Ask F.} and Mouritsen, {Ole G.} and Matthias Weiss",
year = "2005",
month = nov,
day = "30",
doi = "10.1088/0953-8984/17/47/025",
language = "English",
volume = "17",
pages = "S4015--S4024",
journal = "Journal of Physics: Condensed Matter",
issn = "0953-8984",
publisher = "Institute of Physics Publishing Ltd",
number = "47",

}

RIS

TY - JOUR

T1 - Close-up view of the modifications of fluid membranes due to phospholipase A2

AU - Jakobsen, Ask F.

AU - Mouritsen, Ole G.

AU - Weiss, Matthias

PY - 2005/11/30

Y1 - 2005/11/30

N2 - Phospholipases are a class of molecular machines that are involved in the active remodelling processes of biological membranes. These lipases are interfacially activated enzymes and in the specific case of phospholipase A 2 (PLA2) the enzyme catalyses the hydrolysis of di-acyl phospholipids into products of lysolipids and fatty acids, that dramatically change the physical properties of lipid membrane substrates. Using dissipative particle dynamics simulations on a simple coarse-grained bead-spring model of a fluid lipid bilayer in water, the mechanical and diffusive properties of the bilayer in the pure state and after the action of PLA2 have been calculated. It is found that, in response to hydrolysis, the lipid membrane becomes mechanically softened and the various in-plane and trans-bilayer diffusional modes become enhanced. The results compare favourably with available experimental data.

AB - Phospholipases are a class of molecular machines that are involved in the active remodelling processes of biological membranes. These lipases are interfacially activated enzymes and in the specific case of phospholipase A 2 (PLA2) the enzyme catalyses the hydrolysis of di-acyl phospholipids into products of lysolipids and fatty acids, that dramatically change the physical properties of lipid membrane substrates. Using dissipative particle dynamics simulations on a simple coarse-grained bead-spring model of a fluid lipid bilayer in water, the mechanical and diffusive properties of the bilayer in the pure state and after the action of PLA2 have been calculated. It is found that, in response to hydrolysis, the lipid membrane becomes mechanically softened and the various in-plane and trans-bilayer diffusional modes become enhanced. The results compare favourably with available experimental data.

UR - http://www.scopus.com/inward/record.url?scp=27744565097&partnerID=8YFLogxK

U2 - 10.1088/0953-8984/17/47/025

DO - 10.1088/0953-8984/17/47/025

M3 - Journal article

AN - SCOPUS:27744565097

VL - 17

SP - S4015-S4024

JO - Journal of Physics: Condensed Matter

JF - Journal of Physics: Condensed Matter

SN - 0953-8984

IS - 47

ER -

ID: 230985031