Evidence map›Paper›PMID 27992233›Full record

ArticleThe journal of physical chemistry. B2016

Using Multiorder Time-Correlation Functions (TCFs) To Elucidate Biomolecular Reaction Pathways from Microsecond Single-Molecule Fluorescence Experiments.

Carey Phelps, Brett Israels, Morgan C Marsh, Peter H von Hippel, Andrew H Marcus

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Single-molecule FRET methods to study the dynamics of proteins at work.Current opinion in biomedical engineering · 2019
    Article
  10. Article
  11. Studies of DNA breathing in exciton-coupled (iCy3)Proceedings of SPIE--the International Society for Optical Engineering
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Carey PhelpsInstitute of Molecular Biology and Department of Chemistry and Biochemistry and ‡Oregon Center for Optical, Molecular and Quantum Science and Department of Chemistry and Biochemistry, University of Oregon , Eugene, Oregon 97403, United States.
Brett IsraelsInstitute of Molecular Biology and Department of Chemistry and Biochemistry and ‡Oregon Center for Optical, Molecular and Quantum Science and Department of Chemistry and Biochemistry, University of Oregon , Eugene, Oregon 97403, United States.
Morgan C MarshInstitute of Molecular Biology and Department of Chemistry and Biochemistry and ‡Oregon Center for Optical, Molecular and Quantum Science and Department of Chemistry and Biochemistry, University of Oregon , Eugene, Oregon 97403, United States.
Peter H von HippelInstitute of Molecular Biology and Department of Chemistry and Biochemistry and ‡Oregon Center for Optical, Molecular and Quantum Science and Department of Chemistry and Biochemistry, University of Oregon , Eugene, Oregon 97403, United States.
Andrew H MarcusInstitute of Molecular Biology and Department of Chemistry and Biochemistry and ‡Oregon Center for Optical, Molecular and Quantum Science and Department of Chemistry and Biochemistry, University of Oregon , Eugene, Oregon 97403, United States.ORCID 0000-0003-2109-327X

Funding

STRUCTURE AND RELATIONS OF PROTEINS AND NUCLEIC ACIDSR01GM015792 · NIGMS · UNIVERSITY OF OREGON · PI MARCUS, ANDREW HADLEY · 1985 to 2025
$10.2M
MOLECULAR BIOLOGY AND BIOPHYSICST32GM007759 · NIGMS · UNIVERSITY OF OREGON · PI NOLEN, BRADLEY J · 1985 to 2021
$8.5M
Single Molecule Studies of DNA 'Breathing' Fluctuations and their Roles in HelicaF32GM109614 · NIGMS · UNIVERSITY OF OREGON · PI PHELPS, CAREY E · 2014 to 2014
$53k
NIGMS NIH HHS F32 GM109614NIGMS NIH HHS R01 GM015792NIGMS NIH HHS T32 GM007759
6 · The paper itself

Abstract

Recent advances in single-molecule fluorescence imaging have made it possible to perform measurements on microsecond time scales. Such experiments have the potential to reveal detailed information about the conformational changes in biological macromolecules, including the reaction pathways and dynamics of the rearrangements involved in processes, such as sequence-specific DNA "breathing" and the assembly of protein-nucleic acid complexes. Because microsecond-resolved single-molecule trajectories often involve "sparse" data, that is, they contain relatively few data points per unit time, they cannot be easily analyzed using the standard protocols that were developed for single-molecule experiments carried out with tens-of-millisecond time resolution and high "data density." Here, we describe a generalized approach, based on time-correlation functions, to obtain kinetic information from microsecond-resolved single-molecule fluorescence measurements. This approach can be used to identify short-lived intermediates that lie on reaction pathways connecting relatively long-lived reactant and product states. As a concrete illustration of the potential of this methodology for analyzing specific macromolecular systems, we accompany the theoretical presentation with the description of a specific biologically relevant example drawn from studies of reaction mechanisms of the assembly of the single-stranded DNA binding protein of the T4 bacteriophage replication complex onto a model DNA replication fork.

Indexed as

Bacteriophage T4DNA-Binding ProteinsDNA, Single-StrandedFluorescence Resonance Energy TransferFluorescent DyesKineticsOptical ImagingSingle Molecule ImagingStaining and LabelingTime FactorsViral ProteinsDNA-Binding ProteinsDNA, Single-StrandedFluorescent DyesViral Proteins

Identifiers

PMID27992233
PMCPMC5610910

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.