Please note that eDoc will be permanently shut down in the first quarter of 2021!      Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Quick Search
My eDoc
Session History
Support Wiki
Direct access to
document ID:

          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents

ID: 318559.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Diacetylene chelator lipids as support for immobilization and imaging of proteins by atomic force microscopy
Authors:Dorn, I. T.; Hofmann, U. G.; Peltonen, J.; Tampe, R.
Date of Publication (YYYY-MM-DD):1998-08-18
Title of Journal:Langmuir
Issue / Number:17
Start Page:4836
End Page:4842
Review Status:not specified
Audience:Not Specified
Abstract / Description:Chelator Lipids represent a powerful and flexible tool to immobilize, orient, and crystallize histidine-tagged proteins at interfaces. To produce stable two-dimensional polymers that are biofunctional, we synthesized diacetylene lipids carrying a metal-chelating headgroup. These lipids were characterized at the air-water interface with respect to their thermodynamic properties, complex formation, and photopolymerization using film balance techniques combined with epi-fluorescence microscopy. Polymerized monolayers were transferred onto solid supports and reversible binding of histidine-tagged protein/DNA complexes was followed by atomic force microscopy. The versatility of the chelator lipid concept may open the possibility to examine structure and function of proteins or multiprotein assemblies under native conditions and in real time by scanning probe microscopy. [References: 69]
Free Keywords:Scanning probe microscopy; Pentacosadiynoic amide; Artificial membranes; Single-crystals; Molecular films; Monolayers; Interfaces; Binding; Polydiacetylenes; Crystallization.; Physical chemistry/chemical physics.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.