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



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ID: 318469.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Orientation and two-dimensional organization of proteins at chelator lipid interfaces
Authors:Dorn, I. T.; Pawlitschko, K.; Pettinger, S. C.; Tampe, R.
Date of Publication (YYYY-MM-DD):1998
Title of Journal:Biological Chemistry
Volume:379
Issue / Number:8-9
Start Page:1151
End Page:1159
Review Status:not specified
Audience:Not Specified
Abstract / Description:The analysis how proteins interact or assemble with each other in time and space is of central interest. Bio-functionalized interfaces can be applied to study protein-protein interactions in solution or elementary biological processes at membranes. Chelator lipid layers ave well suited for these applications as they specifically bind histidine-tagged fusion proteins and further mimic the two-dimensional world of biological membranes. Here, we used green fluorescent protein (GFP) as a model to study its reversible, functional, and oriented immobilization via histidine-tag at chelator lipid interfaces by various surface sensitive techniques. Taking advantage of the self-organizing properties of chelator lipids, the association and dissociation kinetics, the surface density as well as the organization of the protein in two-dimensional arrays can be controlled. The chelator lipid system can be used for bioanalytical and structural studies as well as to examine recognition processes at membranes. [References: 46]
Free Keywords:Biosensor; Fluorescence; Membranes; Lipid layer; Protein engineering; Supramolecular assemblies.; Surface-plasmon resonance; Histidine-tagged proteins; Green fluorescent protein; Air-water-interface; Reversible immobilization; Recombinant proteins; Monolayers; Bilayers; Binding.; Biochemistry & biophysics.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)
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