Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
By Benjamin Schuler, E. Lipman, W. Eaton. Nature, 2002
836 citations recorded by the source corpus.
Subfields: Biophysics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/9cfda2469ecc8288d3493e52e1ce039c32aac6df
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In Biophysics
In Molecular Biology
- Benjamin Schuler
- W. Eaton
- Ken A. Dill
- J. Hofrichter
- Christopher M. Dobson
- M. Shell
- S. Ozkan
- J. Kubelka
Citations in the corpus
- The protein folding problem. (2008, background): “Furthermore, single-molecule methods are beginning to explore the conformational heterogeneity of folding (23, 133, 166, 194).”
- Protein folding studied by single-molecule FRET. (2008, methodology): “The analysis of the width for the unfolded subpopulation has been a much discussed subject [ 37 ,57] since the first single-molecule folding experiments by Hochstrasser and coworkers [10] and Weiss and coworkers [12], in which the width in excess of that produced by shot noise was attributed to slow”
- Photophysics of Fluorescence Probes for Single Molecule Biophysics and Super-Resolution Imaging (2012, neutral): “Interestingly, such FRET histograms are commonly broader than expected from shot-noise considerations even for simple stiff model systems such as double-stranded DNA (86).”
- The protein folding 'speed limit'. (2004, background): “[31,32,67,70] have measured the variance in the FRET efficiency distribution in 1 ms snapshots of single freely diffusing unfolded protein molecules (CspTm — a 68-residue cold shock protein).”
- Protein folding and misfolding (2003, background): “, some of which can now even be used to follow the behaviour of single molecule”