Lipid protrusions, membrane softness, and enzymatic activity

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Lipid protrusions, membrane softness, and enzymatic activity. / Høyrup, Pernille; Callisen, Thomas H.; Jensen, Morten; Halperin, Avi; Mouritsen, Ole G.

In: Physical Chemistry Chemical Physics, Vol. 6, No. 7, 07.04.2004, p. 1608-1615.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Høyrup, P, Callisen, TH, Jensen, M, Halperin, A & Mouritsen, OG 2004, 'Lipid protrusions, membrane softness, and enzymatic activity', Physical Chemistry Chemical Physics, vol. 6, no. 7, pp. 1608-1615. https://doi.org/10.1039/b314146b

APA

Høyrup, P., Callisen, T. H., Jensen, M., Halperin, A., & Mouritsen, O. G. (2004). Lipid protrusions, membrane softness, and enzymatic activity. Physical Chemistry Chemical Physics, 6(7), 1608-1615. https://doi.org/10.1039/b314146b

Vancouver

Høyrup P, Callisen TH, Jensen M, Halperin A, Mouritsen OG. Lipid protrusions, membrane softness, and enzymatic activity. Physical Chemistry Chemical Physics. 2004 Apr 7;6(7):1608-1615. https://doi.org/10.1039/b314146b

Author

Høyrup, Pernille ; Callisen, Thomas H. ; Jensen, Morten ; Halperin, Avi ; Mouritsen, Ole G. / Lipid protrusions, membrane softness, and enzymatic activity. In: Physical Chemistry Chemical Physics. 2004 ; Vol. 6, No. 7. pp. 1608-1615.

Bibtex

@article{5801bcf71d734377b0447c28c3682459,
title = "Lipid protrusions, membrane softness, and enzymatic activity",
abstract = "The activity of phospholipase A2 on lipid bilayers displays a characteristic lag-burst behavior that has previously been shown to reflect the physical properties of the substrate. It has remained unclear which underlying molecular mechanism is responsible for this phenomenon. We propose here that protrusions of single lipid molecules out of the bilayer plane could provide such a mechanism. The proposal is supported by a combination of atomic-scale molecular dynamics simulations, theory, and experiments that have been performed in order to investigate the relationship between on the one side lipid protrusion modes and mechanical softness of phospholipid bilayers and on the other side the activity of enzymes acting on lipid bilayers composed of different unsaturated lipids. Specifically, our experiments show a correlation between the bilayer bending rigidity and the apparent Arrhenius activation energy extracted from systematic lag-time versus temperature analyses.",
author = "Pernille H{\o}yrup and Callisen, {Thomas H.} and Morten Jensen and Avi Halperin and Mouritsen, {Ole G.}",
year = "2004",
month = apr,
day = "7",
doi = "10.1039/b314146b",
language = "English",
volume = "6",
pages = "1608--1615",
journal = "Physical Chemistry Chemical Physics",
issn = "1463-9076",
publisher = "Royal Society of Chemistry",
number = "7",

}

RIS

TY - JOUR

T1 - Lipid protrusions, membrane softness, and enzymatic activity

AU - Høyrup, Pernille

AU - Callisen, Thomas H.

AU - Jensen, Morten

AU - Halperin, Avi

AU - Mouritsen, Ole G.

PY - 2004/4/7

Y1 - 2004/4/7

N2 - The activity of phospholipase A2 on lipid bilayers displays a characteristic lag-burst behavior that has previously been shown to reflect the physical properties of the substrate. It has remained unclear which underlying molecular mechanism is responsible for this phenomenon. We propose here that protrusions of single lipid molecules out of the bilayer plane could provide such a mechanism. The proposal is supported by a combination of atomic-scale molecular dynamics simulations, theory, and experiments that have been performed in order to investigate the relationship between on the one side lipid protrusion modes and mechanical softness of phospholipid bilayers and on the other side the activity of enzymes acting on lipid bilayers composed of different unsaturated lipids. Specifically, our experiments show a correlation between the bilayer bending rigidity and the apparent Arrhenius activation energy extracted from systematic lag-time versus temperature analyses.

AB - The activity of phospholipase A2 on lipid bilayers displays a characteristic lag-burst behavior that has previously been shown to reflect the physical properties of the substrate. It has remained unclear which underlying molecular mechanism is responsible for this phenomenon. We propose here that protrusions of single lipid molecules out of the bilayer plane could provide such a mechanism. The proposal is supported by a combination of atomic-scale molecular dynamics simulations, theory, and experiments that have been performed in order to investigate the relationship between on the one side lipid protrusion modes and mechanical softness of phospholipid bilayers and on the other side the activity of enzymes acting on lipid bilayers composed of different unsaturated lipids. Specifically, our experiments show a correlation between the bilayer bending rigidity and the apparent Arrhenius activation energy extracted from systematic lag-time versus temperature analyses.

UR - http://www.scopus.com/inward/record.url?scp=2042508368&partnerID=8YFLogxK

U2 - 10.1039/b314146b

DO - 10.1039/b314146b

M3 - Journal article

AN - SCOPUS:2042508368

VL - 6

SP - 1608

EP - 1615

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

SN - 1463-9076

IS - 7

ER -

ID: 230985751