Evidence map›Paper›PMID 17416618›Full record

ArticleBiophysical journal2007

Protein hydrophobic collapse and early folding steps observed in a microfluidic mixer.

Lisa J Lapidus, Shuhuai Yao, Kimberly S McGarrity, David E Hertzog, Emily Tubman, Olgica Bakajin

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 80 citations in OpenAlex.

  1. A Low-Symmetry FeChemistry (Weinheim an der Bergstrasse, Germany) · 2026
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  6. Article
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  11. Translation and folding of single proteins in real time.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Review
  14. How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016
    Review
  15. Review
  16. Article
  17. Article
  18. Fast protein folding kinetics.Quarterly reviews of biophysics · 2014
    Review
  19. Article
  20. 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

6 authors at 2 institutions in 1 country.

Lisa J LapidusDepartment of Physics and Astronomy, Michigan State University, East Lansing, Michigan, USA. lapidus@msu.edu
Shuhuai Yao
Kimberly S McGarrity
David E Hertzog
Emily Tubman
Olgica Bakajin
Lawrence Livermore National Laboratory · USMichigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We demonstrate that the sub-millisecond protein folding process referred to as "collapse" actually consists of at least two separate processes. We observe the UV fluorescence spectrum from naturally occurring tryptophans in three well-studied proteins, cytochrome c, apomyoglobin, and lysozyme, as a function of time in a microfluidic mixer with a dead time of approximately 20 mus. Single value decomposition of the time-dependent spectra reveal two separate processes: 1), a spectral shift which occurs within the mixing time; and 2), a fluorescence decay occurring between approximately 100 and 300 micros. We attribute the first process to hydrophobic collapse and the second process to the formation of the first native tertiary contacts.

Indexed as

Models, ChemicalModels, MolecularProtein FoldingHydrophobic and Hydrophilic InteractionsMicrofluidicsProtein ConformationProtein DenaturationProteinsProteins

Identifiers

PMID17416618
PMCPMC1914423
OpenAlexW2078512978

What OpenQuestion holds

Textmetadata
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.