Incorporation of alpha-Hemolysin in Different Tethered Bilayer Lipid Membrane Architectures.

Incorporation of alpha-Hemolysin in Different Tethered Bilayer Lipid Membrane Architectures. Research Abstract Details 

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Incorporation of alpha-Hemolysin in Different Tethered Bilayer Lipid Membrane Architectures. Abstract Text:

Inga K Vockenroth,Petia P Atanasova,A Toby A Jenkins,Ingo ,Inga K Vockenroth,Petia P Atanasova,A Toby A Jenkins,Ingo Köper,Inga K Vockenroth,Petia P Atanasova,A Toby A Jenkins,Ingo ,

Tethered bilayer lipid membranes are stable solid supported model membrane systems. They can be used to investigate the incorporation and function of membrane proteins. In order to study ion translocation mediated via incorporated proteins, insulating membranes are necessary. The architecture of the membrane can have an important effect on both the electrical properties of the lipid bilayer as well as on the possibility to functionally host proteins. alpha-Hemolysin pores have been functionally incorporated into a tethered bilayer lipid membrane coupled to a gold electrode. The protein incorporation has been monitored optically and electrically and the influence of the molecular structure of the anchor lipids on the insertion properties has been investigated.

Incorporation of alpha-Hemolysin in Different Tethered Bilayer Lipid Membrane Architectures. Publishing Authors By Initials

IK Vockenroth,PP Atanasova,AT Jenkins,I ,IK Vockenroth,PP Atanasova,AT Jenkins,I Köper,IK Vockenroth,PP Atanasova,AT Jenkins,I ,

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Incorporation of alpha-Hemolysin in Different Tethered Bilayer Lipid Membrane Architectures. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Langmuir : the ACS journal of surfaces and colloid

VOLUME: 24

Page Numbers: 496-502

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ISSN: 0743-7463

DAY: 18

MONTH: 12

YEAR: 2007

Incorporation of alpha-Hemolysin in Different Tethered Bilayer Lipid Membrane Architectures. Information

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LANGUAGE: eng

NlmUniqueID: 9882736

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Grant and Affiliation Information for Incorporation of alpha-Hemolysin in Different Tethered Bilayer Lipid Membrane Architectures.

AFFILIATION: Max Planck Institue for Polymer Research, 55128 Mainz, Germany, and University of Bath, Bath BA27AY, UK.

Country: United States

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MEDLINETA: Langmuir

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