• Corpus ID: 21910630

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

@inproceedings{Chemie2009MonitoringPC,
  title={Monitoring Protein Conformations and DNA-Protein Interactions via Single Molecule-FRET Measurements},
  author={Physikalische Chemie and Martina Preiner},
  year={2009}
}
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… 

References

SHOWING 1-10 OF 54 REFERENCES

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

TLDR
DNA can be used as a scaffold for positioning fluorescent proteins, as well as traditional fluorophores, with nanometer accuracy and shows great potential for use in the future of nanobiotechnology.

Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus.

TLDR
This article reviews techniques that allow us to visualize these protein interactions as they occur in living cells and describes the use of FRET microscopy to examine where transcription factors are assembled in the nucleus.

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

TLDR
The TATA-box binding protein (TBP) is required by all three eukaryotic RNA polymerases for the initiation of transcription from most promoters, and two extra classes were identified with intermediate states on a three-step, linear-binding pathway.

Single-molecule three-color FRET.

TLDR
The single-molecule FRET technique is extended to three colors, using the DNA four-way (Holliday) junction as a model system that undergoes two-state conformational fluctuations and is able to show that the acceptor 1 arm moves away from the donor arm at the same time as theacceptor 2 arm approaches the donor hand, marking the first example of observing correlated movements of two different segments of a single molecule.

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

TLDR
It is argued that the orientation parameter is no longer an important issue in the determination of distances determined by FRET using peptides and proteins, and it is suggested that FRET may be a good form of spectroscopy for testing models of F-actin.

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

TLDR
The DNA triple crossover (TX) complex described here extends the set of experimentally characterized building blocks and allows for the presence of reporter strands along the molecular diagonal that can be used to relate the inputs and outputs of DNA-based computation.

Nonequilibrium single molecule protein folding in a coaxial mixer.

TLDR
By transiently populating the unfolded state of Chymotrypsin Inhibitor Protein 2 (CI2) under nonequilibrium in vitro refolding conditions, these results are consistent with previous CI2 mixing results that found evidence for a heterogeneous unfolded state consisting of cis- and trans-proline conformers.

Single-molecule enzymatic dynamics.

TLDR
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

TLDR
A mutational analysis is undertaken that relates the functional prop-erties of GroEL to its crystal structure and finds a highly conserved residue, Asp 87, positioned within a putative nucleotide-binding pocket in the top of the equatorial domain, is essential for ATP hydrolysis and polypeptide release.
...