title: Orientation and two-dimensional organization of proteins at chelator lipid interfaces.
abstract: The analysis how proteins interact or assemble with each other in time and space is of central interest. Biofunctionalized interfaces can be applied to study protein-protein interactions in solution or elementary biological processes at membranes. Chelator lipid layers are 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.
authors.affiliation: Lehrstuhl für Biophysik, Technische Universität München, Garching, Germany.
authors.forename: I T
authors.initials: IT
authors.lastname: Dorn
authors.forename: K
authors.initials: K
authors.lastname: Pawlitschko
authors.forename: S C
authors.initials: SC
authors.lastname: Pettinger
authors.forename: R
authors.initials: R
authors.lastname: Tampé
mesh_terms: D002614:Chelating Agents; D049452:Green Fluorescent Proteins; D007700:Kinetics; D008164:Luminescent Proteins / Q000737:chemistry; D008856:Microscopy, Fluorescence; D010743:Phospholipids / Q000737:chemistry*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D020349:Surface Plasmon Resonance
chemical_list: D002614:Chelating Agents; D008164:Luminescent Proteins; D010743:Phospholipids; D011506:Proteins; D049452:Green Fluorescent Proteins