Striated domain self-organizing ordered assemblies of transmembrane α-helical peptides and lipids in bilayers

Ben de Kruijff; J. Antoinette Killian; D.N. Ganchev; H.A. Rinia; Emma Sparr

doi:10.1515/BC.2006.031

Striated domain self-organizing ordered assemblies of transmembrane α-helical peptides and lipids in bilayers

Ben de Kruijff, J. Antoinette Killian, D.N. Ganchev, H.A. Rinia, Emma Sparr

Physical Chemistry

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

Abstract

This review summarizes the knowledge on striated domains, which are ordered assemblies of transmembrane peptides and lipids under gel-state conditions. The structure, mechanism of function and utility of this system as a model for domain formation is described, resulting in a molecular description of the domains and a discussion on the relevance of these insights for the function/formation and structure of similar domains in biological membranes.

Original language	English
Pages (from-to)	235-241
Journal	Biological Chemistry
Volume	387
Issue number	3
DOIs	https://doi.org/10.1515/BC.2006.031
Publication status	Published - 2006

Subject classification (UKÄ)

Physical Chemistry

Free keywords

lipid-protein interactions
force spectroscopy
bacteriorhodopsin
AFM
self assembly
phase separation

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10.1515/BC.2006.031

Cite this

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abstract = "This review summarizes the knowledge on striated domains, which are ordered assemblies of transmembrane peptides and lipids under gel-state conditions. The structure, mechanism of function and utility of this system as a model for domain formation is described, resulting in a molecular description of the domains and a discussion on the relevance of these insights for the function/formation and structure of similar domains in biological membranes.",

keywords = "lipid-protein interactions, force spectroscopy, bacteriorhodopsin, AFM, self assembly, phase separation",

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AU - Ganchev, D.N.

AU - Rinia, H.A.

AU - Sparr, Emma

PY - 2006

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AB - This review summarizes the knowledge on striated domains, which are ordered assemblies of transmembrane peptides and lipids under gel-state conditions. The structure, mechanism of function and utility of this system as a model for domain formation is described, resulting in a molecular description of the domains and a discussion on the relevance of these insights for the function/formation and structure of similar domains in biological membranes.

KW - lipid-protein interactions

KW - force spectroscopy

KW - bacteriorhodopsin

KW - AFM

KW - self assembly

KW - phase separation

U2 - 10.1515/BC.2006.031

DO - 10.1515/BC.2006.031

M3 - Article

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SN - 1437-4315

VL - 387

SP - 235

EP - 241

JO - Biological Chemistry

JF - Biological Chemistry

IS - 3

ER -

Striated domain self-organizing ordered assemblies of transmembrane α-helical peptides and lipids in bilayers

Abstract

Subject classification (UKÄ)

Free keywords

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