Nano-scale structure in membranes in relation to enzyme action—computer simulation vs. Experiment
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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 journal › Journal article › peer-review
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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