Evidence map›Paper›PMID 26789767›Full record

ArticleBiophysical journal2016

Structure-Based Derivation of Protein Folding Intermediates and Energies from Optical Tweezers.

Aleksander A Rebane, Lu Ma, Yongli Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. A dynamic template complex mediates Munc18-chaperoned SNARE assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022
    Review
  7. Article
  8. Article
  9. Quantitative Models of Lipid Transfer and Membrane Contact Formation.Contact (Thousand Oaks (Ventura County, Calif.)) · 2022
    Article
  10. Article
  11. Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021
    Review
  12. Article
  13. Article
  14. 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
  15. Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.Protein science : a publication of the Protein Society · 2017
    Review
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

3 authors at 1 institution in 1 country.

Aleksander A RebaneDepartment of Cell Biology, School of Medicine, Yale University, New Haven, Connecticut; Integrated Graduate Program in Physical and Engineering Biology, Yale University, New Haven, Connecticut; Department of Physics, Yale University, New Haven, Connecticut.
Lu MaDepartment of Cell Biology, School of Medicine, Yale University, New Haven, Connecticut.
Yongli ZhangDepartment of Cell Biology, School of Medicine, Yale University, New Haven, Connecticut. Electronic address: yongli.zhang@yale.edu.
Yale University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Single-molecule manipulation of SNAREsR01GM093341 · NIGMS · YALE UNIVERSITY · PI ZHANG, YONGLI · 2010 to 2018
$3.1M
NIGMS NIH HHS R01 GM093341NIGMS NIH HHS R01GM093341NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32GM007223
6 · The paper itself

Abstract

Optical tweezers (OTs) measure the force-dependent time-resolved extension of a single macromolecule tethered between two trapped beads. From this measurement, it is possible to determine the folding intermediates, energies, and kinetics of the macromolecule. Previous data analysis generally has used the extension as a reaction coordinate to characterize the observed folding transitions. Despite its convenience, the extension poorly describes folding in the absence of force. Here, we chose the contour length of the unfolded polypeptide as a reaction coordinate and modeled the extensions of protein structures along their predicted folding pathways based on high-resolution structures of the proteins in their native states. We included the extension in our model to calculate the total extensions, energies, and transition rates of the proteins as a function of force. We fit these calculations to the corresponding experimental measurements and obtained the best-fit conformations and energies of proteins in different folding states. We applied our method to analyze single-molecule trajectories of two representative protein complexes responsible for membrane fusion, the HIV-1 glycoprotein 41 and the synaptic SNARE proteins, which involved transitions between two and five states, respectively. Nonlinear fitting of the model to the experimental data revealed the structures of folding intermediates and transition states and their associated energies. Our results demonstrate that the contour length is a useful reaction coordinate to characterize protein folding and that intrinsic extensions of protein structures should be taken into account to properly derive the conformations and energies of protein folding intermediates from single-molecule manipulation experiments.

Indexed as

Optical TweezersProtein FoldingAmino Acid SequenceHIV Envelope Protein gp41Molecular Sequence DataSNARE ProteinsThermodynamicsHIV Envelope Protein gp41SNARE Proteins

Identifiers

PMID26789767
PMCPMC4724646
OpenAlexW2278038000

What OpenQuestion holds

Textmetadata
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Registered trials

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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.