The DOI matches its Crossref record.
Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer
Abstract
Electron transfer is used as a probe for angstrom-scale structural changes in single protein molecules. In a flavin reductase, the fluorescence of flavin is quenched by a nearby tyrosine residue by means of photo-induced electron transfer. By probing the fluorescence lifetime of the single flavin on a photon-by-photon basis, we were able to observe the variation of flavin-tyrosine distance over time. We could then determine the potential of mean force between the flavin and the tyrosine, and a correlation analysis revealed conformational fluctuation at multiple time scales spanning from hundreds of microseconds to seconds. This phenomenon suggests the existence of multiple interconverting conformers related to the fluctuating catalytic reactivity.
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
Cited by
Dynamic personalities of proteins
Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545
Analysis of Single-Molecule FRET Trajectories Using Hidden Markov Modeling
McKinney, S. A., Joo, C., & Ha, T. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.082487 · Cited by 760
Power-law intermittency of single emitters
CICHOS, F., VONBORCZYSKOWSKI, C., & ORRIT, M. (2007) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2007.07.012 · Cited by 301
(2006) · Principles of Fluorescence Spectroscopy · doi:10.1007/978-0-387-46312-4_8 · Cited by 278
Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
Tian, H., Fürstenberg, A., & Huber, T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00084 · Cited by 114
Metadata
- Authors
- Yang, H., Luo, G., Karnchanaphanurach, P., Louie, T.-M., Rech, I., Cova, S., Xun, L., & Xie, X. S.
- Venue
- Science
- Published
- 2003-10-10
- Volume
- 302
- Issue
- 5643
- Pages
- 262-266
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2031573489
- Cited by
- 843
- References
- 0
- FWCI
- 16.51
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer. https://app.cochat.ai/papers/10.1126/science.1086911
- The paper
- Yang, H., Luo, G., Karnchanaphanurach, P., Louie, T.-M., Rech, I., Cova, S., Xun, L., & Xie, X. S. (2003). Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer. Science. https://doi.org/10.1126/science.1086911
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.