Lipids do influence protein function - The hydrophobic matching hypothesis revisited

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Lipids do influence protein function - The hydrophobic matching hypothesis revisited. / Jensen, Morten; Mouritsen, Ole G.

In: Biochimica et Biophysica Acta - Biomembranes, Vol. 1666, No. 1-2, 03.11.2004, p. 205-226.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Jensen, M & Mouritsen, OG 2004, 'Lipids do influence protein function - The hydrophobic matching hypothesis revisited', Biochimica et Biophysica Acta - Biomembranes, vol. 1666, no. 1-2, pp. 205-226. https://doi.org/10.1016/j.bbamem.2004.06.009

APA

Jensen, M., & Mouritsen, O. G. (2004). Lipids do influence protein function - The hydrophobic matching hypothesis revisited. Biochimica et Biophysica Acta - Biomembranes, 1666(1-2), 205-226. https://doi.org/10.1016/j.bbamem.2004.06.009

Vancouver

Jensen M, Mouritsen OG. Lipids do influence protein function - The hydrophobic matching hypothesis revisited. Biochimica et Biophysica Acta - Biomembranes. 2004 Nov 3;1666(1-2):205-226. https://doi.org/10.1016/j.bbamem.2004.06.009

Author

Jensen, Morten ; Mouritsen, Ole G. / Lipids do influence protein function - The hydrophobic matching hypothesis revisited. In: Biochimica et Biophysica Acta - Biomembranes. 2004 ; Vol. 1666, No. 1-2. pp. 205-226.

Bibtex

@article{4373ad6b95744452bb79fbed9d8fe274,
title = "Lipids do influence protein function - The hydrophobic matching hypothesis revisited",
abstract = "A topical review of the current state of lipid-protein interactions is given with focus on the physical interactions between lipids and integral proteins in lipid-bilayer membranes. The concepts of hydrophobic matching and curvature stress are revisited in light of recent data obtained from experimental and theoretical studies which demonstrate that not only do integral proteins perturb the lipids, but the physical state of the lipids does also actively influence protein function. The case of the trans-membrane water-channel protein aquaporin GlpF from E. coli imbedded in lipid-bilayer membranes is discussed in some detail. Numerical data obtained from Molecular Dynamics simulations show on the one side that the lipid bilayer adapts to the channel by a hydrophobic matching condition which reflects the propensity of the lipid molecules for forming curved structures. On the other side, it is demonstrated that the transport function of the channel is modulated by the matching condition and/or the curvature stress in a lipid-specific manner.",
keywords = "Curvature stress, Gramicidin A, Hydrophobic matching, Hydrophobic thickness, Integral membrane protein, Lipid bilayer, Lipid domain, Membrane raft, Protein folding, Protein insertion, Structure-function relationship, Trans-membrane peptide",
author = "Morten Jensen and Mouritsen, {Ole G.}",
year = "2004",
month = nov,
day = "3",
doi = "10.1016/j.bbamem.2004.06.009",
language = "English",
volume = "1666",
pages = "205--226",
journal = "B B A - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "1-2",

}

RIS

TY - JOUR

T1 - Lipids do influence protein function - The hydrophobic matching hypothesis revisited

AU - Jensen, Morten

AU - Mouritsen, Ole G.

PY - 2004/11/3

Y1 - 2004/11/3

N2 - A topical review of the current state of lipid-protein interactions is given with focus on the physical interactions between lipids and integral proteins in lipid-bilayer membranes. The concepts of hydrophobic matching and curvature stress are revisited in light of recent data obtained from experimental and theoretical studies which demonstrate that not only do integral proteins perturb the lipids, but the physical state of the lipids does also actively influence protein function. The case of the trans-membrane water-channel protein aquaporin GlpF from E. coli imbedded in lipid-bilayer membranes is discussed in some detail. Numerical data obtained from Molecular Dynamics simulations show on the one side that the lipid bilayer adapts to the channel by a hydrophobic matching condition which reflects the propensity of the lipid molecules for forming curved structures. On the other side, it is demonstrated that the transport function of the channel is modulated by the matching condition and/or the curvature stress in a lipid-specific manner.

AB - A topical review of the current state of lipid-protein interactions is given with focus on the physical interactions between lipids and integral proteins in lipid-bilayer membranes. The concepts of hydrophobic matching and curvature stress are revisited in light of recent data obtained from experimental and theoretical studies which demonstrate that not only do integral proteins perturb the lipids, but the physical state of the lipids does also actively influence protein function. The case of the trans-membrane water-channel protein aquaporin GlpF from E. coli imbedded in lipid-bilayer membranes is discussed in some detail. Numerical data obtained from Molecular Dynamics simulations show on the one side that the lipid bilayer adapts to the channel by a hydrophobic matching condition which reflects the propensity of the lipid molecules for forming curved structures. On the other side, it is demonstrated that the transport function of the channel is modulated by the matching condition and/or the curvature stress in a lipid-specific manner.

KW - Curvature stress

KW - Gramicidin A

KW - Hydrophobic matching

KW - Hydrophobic thickness

KW - Integral membrane protein

KW - Lipid bilayer

KW - Lipid domain

KW - Membrane raft

KW - Protein folding

KW - Protein insertion

KW - Structure-function relationship

KW - Trans-membrane peptide

UR - http://www.scopus.com/inward/record.url?scp=7244244196&partnerID=8YFLogxK

U2 - 10.1016/j.bbamem.2004.06.009

DO - 10.1016/j.bbamem.2004.06.009

M3 - Review

C2 - 15519316

AN - SCOPUS:7244244196

VL - 1666

SP - 205

EP - 226

JO - B B A - Biomembranes

JF - B B A - Biomembranes

SN - 0005-2736

IS - 1-2

ER -

ID: 230985362