Nano-scale structure in membranes in relation to enzyme action—computer simulation vs. Experiment

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Standard

Nano-scale structure in membranes in relation to enzyme action—computer simulation vs. Experiment. / Høyrup, Pernille; Jørgensen, Kent; Mouritsen, Ole G.

In: Computer Physics Communications, Vol. 147, No. 1-2, 01.08.2002, p. 313-320.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Høyrup, P, Jørgensen, K & Mouritsen, OG 2002, 'Nano-scale structure in membranes in relation to enzyme action—computer simulation vs. Experiment', Computer Physics Communications, vol. 147, no. 1-2, pp. 313-320. https://doi.org/10.1016/S0010-4655(02)00294-1

APA

Høyrup, P., Jørgensen, K., & Mouritsen, O. G. (2002). Nano-scale structure in membranes in relation to enzyme action—computer simulation vs. Experiment. Computer Physics Communications, 147(1-2), 313-320. https://doi.org/10.1016/S0010-4655(02)00294-1

Vancouver

Høyrup P, Jørgensen K, Mouritsen OG. Nano-scale structure in membranes in relation to enzyme action—computer simulation vs. Experiment. Computer Physics Communications. 2002 Aug 1;147(1-2):313-320. https://doi.org/10.1016/S0010-4655(02)00294-1

Author

Høyrup, Pernille ; Jørgensen, Kent ; Mouritsen, Ole G. / Nano-scale structure in membranes in relation to enzyme action—computer simulation vs. Experiment. In: Computer Physics Communications. 2002 ; Vol. 147, No. 1-2. pp. 313-320.

Bibtex

@article{dcb2baf465414c1888653d774f691e14,
title = "Nano-scale structure in membranes in relation to enzyme action—computer simulation vs. Experiment",
abstract = "There is increasing theoretical and experimental evidence indicating that small-scale domain structure and dynamical heterogeneity develop in lipid membranes as a consequence of the the underlying phase transitions and the associated density and composition fluctuations. The relevant coherence lengths are in the nano-meter range. The nano-scale structure is believed to be important for controlling the activity of enzymes, specifically phospholipases, which act at bilayer membranes. We propose here a lattice-gas statistical mechanical model with appropriate dynamics to account for the non-equilibrium action of the enzyme phospholipase A2 which hydrolyses lipid-bilayer substrates. The resulting product molecules are assumed to induce local variations in the membrane interfacial pressure. Monte Carlo simulations of the non-equilibrium properties of the model for one-component as well as binary lipid mixtures show that the enzyme activity is modulated by nano-scale lipid-domain formation in the lipid bilayer and lead to a characteristic lag-burst behavior. The simulations are found to be in semi-quantitative agreement with experimental data.",
keywords = "Computer simulation, Domain formation, Fluctuations, Lipid bilayer, Monte Carlo, Non-equilibrium, Phospholipase A",
author = "Pernille H{\o}yrup and Kent J{\o}rgensen and Mouritsen, {Ole G.}",
year = "2002",
month = "8",
day = "1",
doi = "10.1016/S0010-4655(02)00294-1",
language = "English",
volume = "147",
pages = "313--320",
journal = "Computer Physics Communications",
issn = "0010-4655",
publisher = "Elsevier",
number = "1-2",

}

RIS

TY - JOUR

T1 - Nano-scale structure in membranes in relation to enzyme action—computer simulation vs. Experiment

AU - Høyrup, Pernille

AU - Jørgensen, Kent

AU - Mouritsen, Ole G.

PY - 2002/8/1

Y1 - 2002/8/1

N2 - There is increasing theoretical and experimental evidence indicating that small-scale domain structure and dynamical heterogeneity develop in lipid membranes as a consequence of the the underlying phase transitions and the associated density and composition fluctuations. The relevant coherence lengths are in the nano-meter range. The nano-scale structure is believed to be important for controlling the activity of enzymes, specifically phospholipases, which act at bilayer membranes. We propose here a lattice-gas statistical mechanical model with appropriate dynamics to account for the non-equilibrium action of the enzyme phospholipase A2 which hydrolyses lipid-bilayer substrates. The resulting product molecules are assumed to induce local variations in the membrane interfacial pressure. Monte Carlo simulations of the non-equilibrium properties of the model for one-component as well as binary lipid mixtures show that the enzyme activity is modulated by nano-scale lipid-domain formation in the lipid bilayer and lead to a characteristic lag-burst behavior. The simulations are found to be in semi-quantitative agreement with experimental data.

AB - There is increasing theoretical and experimental evidence indicating that small-scale domain structure and dynamical heterogeneity develop in lipid membranes as a consequence of the the underlying phase transitions and the associated density and composition fluctuations. The relevant coherence lengths are in the nano-meter range. The nano-scale structure is believed to be important for controlling the activity of enzymes, specifically phospholipases, which act at bilayer membranes. We propose here a lattice-gas statistical mechanical model with appropriate dynamics to account for the non-equilibrium action of the enzyme phospholipase A2 which hydrolyses lipid-bilayer substrates. The resulting product molecules are assumed to induce local variations in the membrane interfacial pressure. Monte Carlo simulations of the non-equilibrium properties of the model for one-component as well as binary lipid mixtures show that the enzyme activity is modulated by nano-scale lipid-domain formation in the lipid bilayer and lead to a characteristic lag-burst behavior. The simulations are found to be in semi-quantitative agreement with experimental data.

KW - Computer simulation

KW - Domain formation

KW - Fluctuations

KW - Lipid bilayer

KW - Monte Carlo

KW - Non-equilibrium

KW - Phospholipase A

UR - http://www.scopus.com/inward/record.url?scp=0036681582&partnerID=8YFLogxK

U2 - 10.1016/S0010-4655(02)00294-1

DO - 10.1016/S0010-4655(02)00294-1

M3 - Journal article

AN - SCOPUS:0036681582

VL - 147

SP - 313

EP - 320

JO - Computer Physics Communications

JF - Computer Physics Communications

SN - 0010-4655

IS - 1-2

ER -

ID: 230987236