The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Shot-Noise Limited Single-Molecule FRET Histograms: Comparison between Theory and Experiments
Open accessAbstract
We describe a simple approach and present a straightforward numerical algorithm to compute the best fit shot-noise limited proximity ratio histogram (PRH) in single-molecule fluorescence resonant energy transfer diffusion experiments. The key ingredient is the use of the experimental burst size distribution, as obtained after burst search through the photon data streams. We show how the use of an alternated laser excitation scheme and a correspondingly optimized burst search algorithm eliminates several potential artifacts affecting the calculation of the best fit shot-noise limited PRH. This algorithm is tested extensively on simulations and simple experimental systems. We find that dsDNA data exhibit a wider PRH than expected from shot noise only and hypothetically account for it by assuming a small Gaussian distribution of distances with an average standard deviation of 1.6 A. Finally, we briefly mention the results of a future publication and illustrate them with a simple two-state model system (DNA hairpin), for which the kinetic transition rates between the open and closed conformations are extracted.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Principles of Fluorescence Spectroscopy
Lakowicz, J. R. (1999) · Springer eBooks · doi:10.1007/978-1-4757-3061-6 · Cited by 26,947
Numerical recipes in C: the art of scientific computing
(1993) · Choice Reviews Online · doi:10.5860/choice.30-5638 · Cited by 17,933
Numerical recipes in Pascal: the art of scientific computing
(1990) · Choice Reviews Online · doi:10.5860/choice.27-5158 · Cited by 11,811
Numerical Recipes--The Art of Scientific Computing.
Fritsch, F. N., Press, W. H., Flannery, B. P., Teukolsky, S. A., & Vetterling, W. T. (1988) · Mathematics of Computation · doi:10.2307/2007938 · Cited by 4,845
Numerical Recipes in C: The Art of Scientific Computing.
Birchenhall, C., Press, W. H., Teukolsky, S. A., Vetterling, W. T., & Flannery, B. P. (1994) · The Economic Journal · doi:10.2307/2234664 · Cited by 4,355
Fluorescence Spectroscopy of Single Biomolecules
Weiss, S. (1999) · Science · doi:10.1126/science.283.5408.1676 · Cited by 2,046
Self-citationEnergy transfer: a spectroscopic ruler.
Stryer, L., & Haugland, R. P. (1967) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.58.2.719 · Cited by 1,957
Ten years of tension: single-molecule DNA mechanics
Bustamante, C., Bryant, Z., & Smith, S. B. (2003) · Nature · doi:10.1038/nature01405 · Cited by 1,303
Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
Schuler, B., Lipman, E. A., & Eaton, W. A. (2002) · Nature · doi:10.1038/nature01060 · Cited by 921
Single-molecule imaging of EGFR signalling on the surface of living cells
Sako, Y., Minoghchi, S., & Yanagida, T. (2000) · Nature Cell Biology · doi:10.1038/35004044 · Cited by 890
Cited by
Intrinsic motions along an enzymatic reaction trajectory
Henzler-Wildman, K. A., Thai, V., Lei, M., Ott, M., Wolf-Watz, M., Fenn, T., Pozharski, E., Wilson, M. A., Petsko, G. A., Karplus, M., et al. (2007) · Nature · doi:10.1038/nature06410 · Cited by 887
Protein folding studied by single-molecule FRET
Schuler, B., & Eaton, W. A. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.12.003 · Cited by 697
Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study
Hellenkamp, B., Schmid, S., Doroshenko, O., Opanasyuk, O., Kühnemuth, R., Rezaei Adariani, S., Ambrose, B., Aznauryan, M., Barth, A., Birkedal, V., et al. (2018) · Nature Methods · doi:10.1038/s41592-018-0085-0 · Cited by 519
A toolkit and benchmark study for FRET-restrained high-precision structural modeling
Kalinin, S., Peulen, T., Sindbert, S., Rothwell, P. J., Berger, S., Restle, T., Goody, R. S., Gohlke, H., & Seidel, C. A. M. (2012) · Nature Methods · doi:10.1038/nmeth.2222 · Cited by 434
Accurate Single-Molecule FRET Studies Using Multiparameter Fluorescence Detection
Sisamakis, E., Valeri, A., Kalinin, S., Rothwell, P. J., & Seidel, C. A. M. (2010) · Methods in Enzymology · doi:10.1016/s0076-6879(10)75018-7 · Cited by 268
Succinylation of H3K122 destabilizes nucleosomes and enhances transcription
Zorro Shahidian, L., Haas, M., Le Gras, S., Nitsch, S., Mourão, A., Geerlof, A., Margueron, R., Michaelis, J., Daujat, S., & Schneider, R. (2021) · The EMBO Reports · doi:10.15252/embr.202051009 · Cited by 92
Dynamic action of the Sec machinery during initiation, protein translocation and termination.
Fessl, T., Watkins, D., Oatley, P., Allen, W. J., Corey, R. A., Horne, J., Baldwin, S. A., Radford, S. E., Collinson, I., & Tuma, R. (2018) · eLife · doi:10.7554/elife.35112 · Cited by 56
Wörle, E., Newman, A., D’Silva, J., Burgio, G., & Grohmann, D. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac767 · Cited by 32
Metadata
- Authors
- Nir, E., Michalet, X., Hamadani, K. M., Laurence, T. A., Neuhauser, D., Kovchegov, Y., & Weiss, S.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-10-19
- Volume
- 110
- Issue
- 44
- Pages
- 22103-22124
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W1996762013
- Cited by
- 314
- References
- 53
- FWCI
- 7.84
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.