Share This Author
Fluorescence and spin properties of defects in single digit nanodiamonds.
Stable photoluminescence and high-contrast optically detected electron spin resonance (ODESR) from single nitrogen-vacancy (NV) defect centers created within ultrasmall, disperse nanodiamonds of radius less than 4 nm conclude that despite the tiny size of these nanod diamonds the photoactive nitrogen-Vacancy color centers retain their bulk properties to the benefit of numerous exciting potential applications in photonics, biomedical labeling, and imaging.
Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase
- M. Diez, B. Zimmermann, P. Gräber
- Chemistry, BiologyNature Structural &Molecular Biology
- 1 February 2004
This work incorporated double-labeled F0F1-ATP synthases from Escherichia coli into liposomes and measured single-molecule fluorescence resonance energy transfer (FRET) during ATP synthesis and hydrolysis.
Sequential bottom-up assembly of mechanically stabilized synthetic cells by microfluidics.
A high-throughput microfluidic method is presented to generate stable, defined sized liposomes termed 'droplet-stabilized giant unilamellar vesicles (dsGUVs)', and the enhanced stability of dsGUVs enables the sequential loading of these compartments with biomolecules, namely purified transmembrane and cytoskeleton proteins by microfluidity pico-injection technology.
Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Gö1: Implications of nucleotide-binding differences in the major A1Ao subunits A and B.
Distances between the b-subunits in the tether domain of F(0)F(1)-ATP synthase from E. coli.
Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding
Stepwise rotation of the γ‐subunit of EF0F1‐ATP synthase observed by intramolecular single‐molecule fluorescence resonance energy transfer 1
Dynamic Ligand-induced Conformational Rearrangements in P-glycoprotein as Probed by Fluorescence Resonance Energy Transfer Spectroscopy*
- Brandy Verhalen, S. Ernst, M. Börsch, S. Wilkens
- Biology, ChemistryThe Journal of Biological Chemistry
- 15 November 2011
The two nucleotide binding domains are found to be in close association during the catalytic cycle as determined by fluorescence spectroscopy, suggesting the presence of at least three major conformations of the NBDs during catalysis.
Movements of the ε‐subunit during catalysis and activation in single membrane‐bound H+‐ATP synthase
It is concluded that the active–inactive transition was associated with a conformational change of ε within the central stalk within F0F1‐ATP synthases, which catalyze proton transport‐coupled ATP synthesis in bacteria, chloroplasts, and mitochondria.
36° step size of proton‐driven c‐ring rotation in FoF1‐ATP synthase
Using single‐molecule fluorescence resonance energy transfer, this work provides the first experimental determination of a 36° sequential stepping mode of the c‐ring during ATP synthesis.