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The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Single-Molecule Fluorescence Experiments Determine Protein Folding Transition Path Times

Open access
Chung, Hoi Sung, McHale, Kevin, Louis, John M., Eaton, William A.·2012·Science

Abstract

A Fraction of Folding: An energy barrier has to be crossed as a protein transforms between folded and unfolded states. Molecular dynamic simulations have observed sharp transitions, with barrier crossing times of less than a microsecond, a fraction of the total folding time; however, this time range has been inaccessible to single-molecule experiments. Chung et al. (p. 981 ) described single-molecule fluorescence experiments that allowed measurement of the transition-path time for a fast-folding protein and to reduce the upper bound for a slow-folding protein. Although the folding rates differed by a factor of 10,000, the transition-path times differ by less than a factor of 5, pointing to energy landscape theory for the explanation.

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Crossref · 10.1126/science.1215768

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Metadata

Authors
Chung, H. S., McHale, K., Louis, J. M., & Eaton, W. A.
Venue
Science
Published
2012-02-24
Volume
335
Issue
6071
Pages
981-984
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2150614072
Cited by
414
References
32
FWCI
15.22
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Single-Molecule Fluorescence Experiments Determine Protein Folding Transition Path Times. https://app.cochat.ai/papers/10.1126/science.1215768
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Chung, H. S., McHale, K., Louis, J. M., & Eaton, W. A. (2012). Single-Molecule Fluorescence Experiments Determine Protein Folding Transition Path Times. Science. https://doi.org/10.1126/science.1215768

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