Evidence map›Paper›PMID 28742962›Full record

ArticleAnalytical chemistry2017

Characterization of Intramolecular Interactions of Cytochrome c Using Hydrogen-Deuterium Exchange-Trapped Ion Mobility Spectrometry-Mass Spectrometry and Molecular Dynamics.

Juan Camilo Molano-Arevalo, Kevin Jeanne Dit Fouque, Khoa Pham, Jaroslava Miksovska, Mark E Ridgeway, Melvin A Park, Francisco Fernandez-Lima

Abstract read
In one paragraph

Article in Analytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Collision-Induced Unfolding of High-Journal of the American Society for Mass Spectrometry · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Structural Heterogeneity of Human Histone H2A.1.The journal of physical chemistry. B · 2021
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Evidence of Cis/Trans-Isomerization at Pro7/Pro16 in the Lasso Peptide Microcin J25.Journal of the American Society for Mass Spectrometry · 2019
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. 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

7 authors.

Juan Camilo Molano-ArevaloDepartment of Chemistry and Biochemistry, Florida International University , Miami, Florida 33199, United States.
Kevin Jeanne Dit FouqueDepartment of Chemistry and Biochemistry, Florida International University , Miami, Florida 33199, United States.
Khoa PhamDepartment of Chemistry and Biochemistry, Florida International University , Miami, Florida 33199, United States.
Jaroslava MiksovskaDepartment of Chemistry and Biochemistry, Florida International University , Miami, Florida 33199, United States.ORCID 0000-0002-0385-9457
Mark E RidgewayBruker Daltonics, Inc. , Billerica, Massachusetts 01821, United States.
Melvin A ParkBruker Daltonics, Inc. , Billerica, Massachusetts 01821, United States.
Francisco Fernandez-LimaDepartment of Chemistry and Biochemistry, Florida International University , Miami, Florida 33199, United States.ORCID 0000-0002-1283-4390

Funding

Mass Spectrometry based molecular imaging of native biological nanodomainsR00GM106414 · NIGMS · FLORIDA INTERNATIONAL UNIVERSITY · PI FERNANDEZ-LIMA, FRANCISCO · 2012 to 2014
$731k
NIGMS NIH HHS R00 GM106414
6 · The paper itself

Abstract

Globular proteins, such as cytochrome c (cyt c), display an organized native conformation, maintained by a hydrogen bond interaction network. In the present work, the structural interrogation of kinetically trapped intermediates of cyt c was performed by correlating the ion-neutral collision cross section (CCS) and charge state with the starting solution conditions and time after desolvation using collision induced activation (CIA), time-resolved hydrogen/deuterium back exchange (HDX) and trapped ion mobility spectrometry-mass spectrometry (TIMS-MS). The high ion mobility resolving power of the TIMS analyzer allowed the identification of new ion mobility bands, yielding a total of 63 mobility bands over the +6 to +21 charge states and 20 mobility bands over the -5 to -10 charge states. Mobility selected HDX rates showed that for the same charge state, conformers with larger CCS present faster HDX rates in both positive and negative ion mode, suggesting that the charge sites and neighboring exchange sites on the accessible surface area define the exchange rate regardless of the charge state. Complementary molecular dynamic simulations permitted the generation of candidate structures and a mechanistic model of the folding transitions from native (N) to molten globule (MG) to kinetic intermediates (U) pathways. Our results suggest that cyt c major structural unfolding is associated with the distancing of the N- and C-terminal helices and subsequent solvent exposure of the hydrophobic, heme-containing cavity.

Indexed as

AnimalsCytochromes cDeuterium Exchange MeasurementHorsesIon Mobility SpectrometryMass SpectrometryMolecular Dynamics SimulationProtein ConformationProtein UnfoldingCytochromes c

Identifiers

PMID28742962
PMCPMC5653375

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.