Evidence map›Paper›PMID 25140430›Full record

ArticleBiophysical journal2014

Complex pathways in folding of protein G explored by simulation and experiment.

Lisa J Lapidus, Srabasti Acharya, Christian R Schwantes, Ling Wu, Diwakar Shukla, Michael King, Stephen J DeCamp, Vijay S Pande

Abstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. AlphaFold2bioRxiv : the preprint server for biology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Modeling molecular kinetics with tICA and the kernel trick.Journal of chemical theory and computation · 2015
    Article
  17. 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

8 authors.

Lisa J LapidusDepartment of Physics and Astronomy, Michigan State University, East Lansing, Michigan. Electronic address: lapidus@msu.edu.
Srabasti AcharyaDepartment of Physics and Astronomy, Michigan State University, East Lansing, Michigan.
Christian R SchwantesDepartment of Chemistry, Stanford University, Stanford, California.
Ling WuDepartment of Physics and Astronomy, Michigan State University, East Lansing, Michigan.
Diwakar ShuklaDepartment of Chemistry, Stanford University, Stanford, California; Simbios Program, Stanford University, Stanford, California.
Michael KingDepartment of Physics and Astronomy, Michigan State University, East Lansing, Michigan.
Stephen J DeCampDepartment of Physics and Astronomy, Michigan State University, East Lansing, Michigan.
Vijay S PandeDepartment of Chemistry, Stanford University, Stanford, California; Simbios Program, Stanford University, Stanford, California; Department of Structural Biology, Stanford University, Stanford, California; Biophysics Program, Stanford University, Stanford, California; Department of Computer Science, Stanford University, Stanford, California.

Funding

Physics-based Simulation of Biological Structures(RMI)U54GM072970 · NIGMS · STANFORD UNIVERSITY · PI ALTMAN, RUSS BIAGIO · 2004 to 2013
$33.5M
Topology, nucleation, and the protein folding barrierR01GM062868 · NIGMS · STANFORD UNIVERSITY · PI PANDE, VIJAY S · 2002 to 2018
$5.5M
NIGMS NIH HHS R01 GM062868NIGMS NIH HHS R01-GM062868NIGMS NIH HHS U54 GM07297NIGMS NIH HHS U54 GM072970
6 · The paper itself

Abstract

The B1 domain of protein G has been a classic model system of folding for decades, the subject of numerous experimental and computational studies. Most of the experimental work has focused on whether the protein folds via an intermediate, but the evidence is mostly limited to relatively slow kinetic observations with a few structural probes. In this work we observe folding on the submillisecond timescale with microfluidic mixers using a variety of probes including tryptophan fluorescence, circular dichroism, and photochemical oxidation. We find that each probe yields different kinetics and compare these observations with a Markov State Model constructed from large-scale molecular dynamics simulations and find a complex network of states that yield different kinetics for different observables. We conclude that there are many folding pathways before the final folding step and that these paths do not have large free energy barriers.

Indexed as

Protein FoldingCircular DichroismEscherichia coliFluorescenceGTP-Binding ProteinsKineticsMarkov ChainsMicrofluidic Analytical TechniquesMolecular Dynamics SimulationOxidants, PhotochemicalPhotochemical ProcessesTime FactorsTryptophanGTP-Binding ProteinsOxidants, PhotochemicalTryptophan

Identifiers

PMID25140430
PMCPMC4147789

What OpenQuestion holds

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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.