Evidence map›Paper›PMID 21190388›Full record

ArticleBiochemistry2011

Manifestations of native topology in the denatured state ensemble of Rhodopseudomonas palustris cytochrome c'.

Tanveer A Dar, R Dustin Schaeffer, Valerie Daggett, Bruce E Bowler

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Shared unfolding pathways of unrelated immunoglobulin-like β-sandwich proteins.Protein engineering, design & selection : PEDS · 2019
    Article
  6. Review
  7. Article
  8. Article
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  11. Article
  12. Article
  13. Article
  14. Residual structure in unfolded proteins.Current opinion in structural biology · 2012
    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

4 authors at 2 institutions in 2 countries.

Tanveer A DarDepartment of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, Montana 59812, United States.
R Dustin Schaeffer
Valerie Daggett
Bruce E Bowler
University of Montana · USBioengineering Center · RU

Funding

MOLECULAR DYNAMICS SIMULATIONS OF PROTEIN UNFOLDINGR01GM050789 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAGGETT, VALERIE D · 2000 to 2014
$3.9M
Conformational Properties of Protein Denatured StatesR01GM074750 · NIGMS · UNIVERSITY OF MONTANA · PI BOWLER, BRUCE E · 2005 to 2009
$947k
NIGMS NIH HHS R01 GM050789NIGMS NIH HHS R01GM050789NIGMS NIH HHS R01 GM074750NIGMS NIH HHS R01GM074750
6 · The paper itself

Abstract

To provide insight into the role of local sequence in the nonrandom coil behavior of the denatured state, we have extended our measurements of histidine-heme loop formation equilibria for cytochrome c' to 6 M guanidine hydrochloride. We observe that there is some reduction in the scatter about the best fit line of loop stability versus loop size data in 6 M versus 3 M guanidine hydrochloride, but the scatter is not eliminated. The scaling exponent, ν(3), of 2.5 ± 0.2 is also similar to that found previously in 3 M guanidine hydrochloride (2.6 ± 0.3). Rates of histidine-heme loop breakage in the denatured state of cytochrome c' show that some histidine-heme loops are significantly more persistent than others at both 3 and 6 M guanidine hydrochloride. Rates of histidine-heme loop formation more closely approximate random coil behavior. This observation indicates that heterogeneity in the denatured state ensemble results mainly from contact persistence. When mapped onto the structure of cytochrome c', the histidine-heme loops with slow breakage rates coincide with chain reversals between helices 1 and 2 and between helices 2 and 3. Molecular dynamics simulations of the unfolding of cytochrome c' at 498 K show that these reverse turns persist in the unfolded state. Thus, these portions of the primary structure of cytochrome c' set up the topology of cytochrome c' in the denatured state, predisposing the protein to fold efficiently to its native structure.

Indexed as

Bacterial ProteinsCytochromes c'GuanidineHydrogen-Ion ConcentrationKineticsModels, MolecularProtein ConformationProtein DenaturationProtein FoldingRhodopseudomonasBacterial ProteinsCytochromes c'Guanidine

Identifiers

PMID21190388
PMCPMC3329124
OpenAlexW2313059659

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.