Evidence map›Paper›PMID 19436489›Full record

ArticleHFSP journal2008

Ruggedness in the folding landscape of protein L.

Steven A Waldauer, Olgica Bakajin, Terry Ball, Yujie Chen, Stephen J Decamp, Michaela Kopka, Marcus Jäger, Vijay R Singh, William J Wedemeyer, Shimon Weiss and 2 more

Abstract read
In one paragraph

Article in HFSP journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016
    Review
  3. Article
  4. Fast protein folding kinetics.Quarterly reviews of biophysics · 2014
    Review
  5. Article
  6. Microfluidic mixers for studying protein folding.Journal of visualized experiments : JoVE · 2012
    Article
  7. How, when and why proteins collapse: the relation to folding.Current opinion in structural biology · 2012
    Review
  8. Taming the complexity of protein folding.Current opinion in structural biology · 2011
    Review
  9. Extremely slow intramolecular diffusion in unfolded protein L.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  10. Protein folded states are kinetic hubs.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  11. Article
  12. 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

12 authors.

Steven A Waldauer
Olgica Bakajin
Terry Ball
Yujie Chen
Stephen J Decamp
Michaela Kopka
Marcus Jäger
Vijay R Singh
William J Wedemeyer
Shimon Weiss
Shuhuai Yao
Lisa J Lapidus

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By exploring the folding pathways of the B1 domain of protein L with a series of equilibrium and rapid kinetic experiments, we have found its unfolded state to be more complex than suggested by two-state folding models. Using an ultrarapid mixer to initiate protein folding within approximately 2-4 microseconds, we observe folding kinetics by intrinsic tryptophan fluorescence and fluorescence resonance energy transfer. We detect at least two processes faster than 100 mus that would be hidden within the burst phase of a stopped-flow instrument measuring tryptophan fluorescence. Previously reported measurements of slow intramolecular diffusion are commensurate with the slower of the two observed fast phases. These results suggest that a multidimensional energy landscape is necessary to describe the folding of protein L, and that the dynamics of the unfolded state is dominated by multiple small energy barriers.

Identifiers

PMID19436489
PMCPMC2645578

What OpenQuestion holds

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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.