Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds.

@article{Nettels2008UnfoldedPA,
  title={Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds.},
  author={Daniel Nettels and Armin Hoffmann and Benjamin Schuler},
  journal={The journal of physical chemistry. B},
  year={2008},
  volume={112 19},
  pages={6137-46}
}
Single-molecule fluorescence spectroscopy and correlation methods are finding increasing applications in the investigation of biomolecular dynamics, especially together with Förster resonance energy transfer (FRET). Here, we use the combination of start-stop experiments and classical fluorescence correlation spectroscopy (FCS) to obtain complete intensity auto- and cross-correlation functions from picoseconds to seconds for investigating the dynamics of unfolded proteins and peptides. In… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 44 extracted citations

References

Publications referenced by this paper.
Showing 1-5 of 5 references

proteins: The dependence of fluorescence resonance energy transfer (FRET)-derived protein reconfiguration times on the location of the FRET probes

  • D. Nettels, I. V. Gopich, A. Hoffmann, B. Schuler
  • J. Chem. Phys
  • 2010

Antibunching and Rotational Diffusion in FCS

  • Ü. Mets
  • Fluorescence Correlation Spectroscopy

Cross - Correlation Analysis in FCS

  • P. Schwille
  • Fluorescence Correlation Spectroscopy

Similar Papers

Loading similar papers…