Evidence map›Paper›PMID 32569525›Full record

ReviewAnnual review of biochemistry2020

Single-Molecule Studies of Protein Folding with Optical Tweezers.

Carlos Bustamante, Lisa Alexander, Kevin Maciuba, Christian M Kaiser

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
17.2field-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

97 citing papers in PubMed, 201 citations in OpenAlex.

  1. Review
  2. How proteins fold.Nature reviews. Molecular cell biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. The Minimal Folding Motif of the Repeat-in-Toxin Domain of Adenylate Cyclase Toxin.Langmuir : the ACS journal of surfaces and colloids · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

37 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Carlos BustamanteDepartment of Molecular and Cell Biology, Department of Physics, Howard Hughes Medical Institute, and Kavli Energy NanoScience Institute, University of California, Berkeley, California 94720, USA; email: carlosb@berkeley.edu.
Lisa AlexanderDepartment of Chemistry, University of California, Berkeley, California 94720, USA.
Kevin MaciubaCell, Molecular, Developmental Biology, and Biophysics Graduate Program, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Christian M KaiserDepartment of Biology and Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA; email: kaiser@jhu.edu.
Johns Hopkins University · USHoward Hughes Medical Institute · USUniversity of California, Berkeley · US

Funding

CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
THE PHYSICAL CHEMISTRY OF NUCLEIC ACIDSR01GM032543 · NIGMS · UNIVERSITY OF OREGON · PI CARLOS Jose BUSTAMANTE · 1985 to 2026
$6.4M
Mechanisms of Viral DNA PackagingR01GM071552 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BUSTAMANTE, CARLOS JOSE · 2004 to 2015
$4.7M
Folding and Chaperone Interactions of Multi-domain ProteinsR01GM121567 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HILSER, VINCENT J. · 2017 to 2025
$3.2M
NIGMS NIH HHS R01 GM032543NIGMS NIH HHS R01 GM071552NIGMS NIH HHS R01 GM121567NIGMS NIH HHS T32 GM007231
6 · The paper itself

Abstract

Manipulation of individual molecules with optical tweezers provides a powerful means of interrogating the structure and folding of proteins. Mechanical force is not only a relevant quantity in cellular protein folding and function, but also a convenient parameter for biophysical folding studies. Optical tweezers offer precise control in the force range relevant for protein folding and unfolding, from which single-molecule kinetic and thermodynamic information about these processes can be extracted. In this review, we describe both physical principles and practical aspects of optical tweezers measurements and discuss recent advances in the use of this technique for the study of protein folding. In particular, we describe the characterization of folding energy landscapes at high resolution, studies of structurally complex multidomain proteins, folding in the presence of chaperones, and the ability to investigate real-time cotranslational folding of a polypeptide.

Indexed as

Optical TweezersProtein BiosynthesisEscherichia coliHumansKineticsMicroscopy, Atomic ForceModels, MolecularMolecular ChaperonesProtein BindingProtein FoldingProtein Interaction Domains and MotifsProteomeProteostasisRibosomesThermodynamicsMolecular ChaperonesProteomeco-translational foldingmolecular chaperonesoptical tweezersprotein folding

Identifiers

PMID32569525
PMCPMC7487275
OpenAlexW3036620924

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.