Evidence map›Paper›PMID 29709179›Full record

ArticleThe journal of physical chemistry. B2018

Probing Cytochrome c Folding Transitions upon Phototriggered Environmental Perturbations Using Time-Resolved X-ray Scattering.

Dolev Rimmerman, Denis Leshchev, Darren J Hsu, Jiyun Hong, Baxter Abraham, Robert Henning, Irina Kosheleva, Lin X Chen

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

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  12. Heterogeneous folding and stretched kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Protein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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 at 3 institutions in 1 country.

Dolev RimmermanDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.
Denis LeshchevDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.
Darren J HsuDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.
Jiyun HongDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.
Baxter AbrahamDepartment of Chemistry and Biochemistry , University of Delaware , Newark , Delaware 19716 , United States.
Robert HenningCenter for Advanced Radiation Sources , The University of Chicago , Chicago , Illinois 60637 , United States.
Irina KoshelevaCenter for Advanced Radiation Sources , The University of Chicago , Chicago , Illinois 60637 , United States.
Lin X ChenDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.ORCID 0000-0002-8450-6687
Northwestern University · USUniversity of Chicago · USUniversity of Delaware · US

Funding

Capturing Transient Protein Structures on Multiple Spatial and Temporal ScalesR01GM115761 · NIGMS · NORTHWESTERN UNIVERSITY · PI CHEN, LIN X · 2015 to 2023
$3.0M
BioCARS: A Synchrotron Structure Biology ResourceR24GM111072 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2013 to 2016
$2.3M
NIGMS NIH HHS R01 GM115761NIGMS NIH HHS R24 GM111072
6 · The paper itself

Abstract

Direct tracking of protein structural dynamics during folding-unfolding processes is important for understanding the roles of hierarchic structural factors in the formation of functional proteins. Using cytochrome c (cyt c) as a platform, we investigated its structural dynamics during folding processes triggered by local environmental changes (i.e., pH or heme iron center oxidation/spin/ligation states) with time-resolved X-ray solution scattering measurements. Starting from partially unfolded cyt c, a sudden pH drop initiated by light excitation of a photoacid caused a structural contraction in microseconds, followed by active site restructuring and unfolding in milliseconds. In contrast, the reduction of iron in the heme via photoinduced electron transfer did not affect conformational stability at short timescales (<1 ms), despite active site coordination geometry changes. These results demonstrate how different environmental perturbations can change the nature of interaction between the active site and protein conformation, even within the same metalloprotein, which will subsequently affect the folding structural dynamics.

Indexed as

LightProtein FoldingAnimalsCytochromes cHemeModels, MolecularProtein ConformationProtein UnfoldingTime FactorsX-Ray DiffractionCytochromes cHeme

Identifiers

PMID29709179
PMCPMC6503524
OpenAlexW2802102944

What OpenQuestion holds

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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.