Evidence map›Paper›PMID 27844436›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2017

Single-Molecule Protein Folding Experiments Using High-Precision Optical Tweezers.

Junyi Jiao, Aleksander A Rebane, Lu Ma, Yongli Zhang

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
18.9field-weighted citation impact, top 1% of its field
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

22 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. A dynamic template complex mediates Munc18-chaperoned SNARE assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Review
  9. Article
  10. Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Munc13-1 MUN domain and Munc18-1 cooperatively chaperone SNARE assembly through a tetrameric complex.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Article
  17. Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Junyi JiaoDepartment of Cell Biology, School of Medicine and Integrated Graduate Program in Physical and Engineering Biology, Yale University, 333 Cedar Street, New Haven, CT, 06520, USA.
Aleksander A RebaneDepartment of Cell Biology, School of Medicine and Integrated Graduate Program in Physical and Engineering Biology, Yale University, 333 Cedar Street, New Haven, CT, 06520, USA.
Lu MaDepartment of Cell Biology, School of Medicine, Yale University, 333 Cedar Street, New Haven, CT, 06520, USA.
Yongli ZhangDepartment of Cell Biology, School of Medicine, Yale University, 333 Cedar Street, New Haven, CT, 06520, USA. yongli.zhang@yale.edu.
Yale University · US

Funding

Single-molecule manipulation of SNAREsR01GM093341 · NIGMS · YALE UNIVERSITY · PI ZHANG, YONGLI · 2010 to 2018
$3.1M
NIGMS NIH HHS R01 GM093341
6 · The paper itself

Abstract

How proteins fold from linear chains of amino acids to delicate three-dimensional structures remains a fundamental biological problem. Single-molecule manipulation based on high-resolution optical tweezers (OT) provides a powerful approach to study protein folding with unprecedented spatiotemporal resolution. In this method, a single protein or protein complex is tethered between two beads confined in optical traps and pulled. Protein unfolding induced by the mechanical force is counteracted by the spontaneous folding of the protein, reaching a dynamic equilibrium at a characteristic force and rate. The transition is monitored by the accompanying extension change of the protein and used to derive conformations and energies of folding intermediates and their associated transition kinetics. Here, we provide general strategies and detailed protocols to study folding of proteins and protein complexes using optical tweezers, including sample preparation, DNA-protein conjugation and methods of data analysis to extract folding energies and rates from the single-molecule measurements.

Indexed as

Optical TweezersProtein FoldingDNA-Binding ProteinsMarkov ChainsMicrofluidicsModels, MolecularMultiprotein ComplexesProtein ConformationProteinsSingle Molecule ImagingSNARE ProteinsDNA-Binding ProteinsMultiprotein ComplexesProteinsSNARE ProteinsEnergy landscapegp41Hidden Markov modelingOptical tweezersProtein foldingSingle-molecule manipulationSNARE assemblySNARE proteins

Identifiers

PMID27844436
PMCPMC5508109
OpenAlexW2555236069

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.