• Corpus ID: 21910630

Monitoring Protein Conformations and DNA-Protein Interactions via Single Molecule-FRET Measurements

  title={Monitoring Protein Conformations and DNA-Protein Interactions via Single Molecule-FRET Measurements},
  author={Physikalische Chemie and Martina Preiner},
Observing concrete steps and dynamics of biochemical processes is nowadays an important tool to discover the secrets of life. In many cases, fluorescence microscopy and spectroscopy on single molecules enable these kinds of investigations. Measurements on single molecules are highly facilitated by confocal fluorescence spectroscopy. By combining single molecule measurements with Forster resonance energy transfer (FRET), snapshots of the distribution of conformational states of a biomolecule are… 



A single-molecule Förster resonance energy transfer analysis of fluorescent DNA-protein conjugates for nanobiotechnology.

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Stepwise bending of DNA by a single TATA-box binding protein.

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Single-molecule three-color FRET.

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Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor.

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Construction, analysis, ligation, and self-assembly of DNA triple crossover complexes

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Nonequilibrium single molecule protein folding in a coaxial mixer.

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A molecular memory phenomenon, in which an enzymatic turnover was not independent of its previous turnovers because of a slow fluctuated of protein conformation, was evidenced by spontaneous spectral fluctuation of FAD.

Residues in chaperonin GroEL required for polypeptide binding and release

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