Evidence map›Paper›PMID 26032343›Full record

ArticleProtein science : a publication of the Protein Society2015

Electron-capture dissociation and ion mobility mass spectrometry for characterization of the hemoglobin protein assembly.

Weidong Cui, Hao Zhang, Robert E Blankenship, Michael L Gross

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

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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

4 authors.

Weidong CuiDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri, 63130.
Hao ZhangDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri, 63130.
Robert E BlankenshipDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri, 63130.
Michael L GrossDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri, 63130.

Funding

TrainingP41GM103422 · NIGMS · WASHINGTON UNIVERSITY · PI YARASHESKI, KEVIN E · 2012 to 2019
$12.0M
NIGMS NIH HHS 8 P41 GM103422
6 · The paper itself

Abstract

Native spray has the potential to probe biophysical properties of protein assemblies. Here we report an investigation using both ECD top-down sequencing with an FTICR mass spectrometer and ion mobility (IM) measurements on a Q-TOF to investigate the collisionally induced unfolding of a native-like heterogeneous tetrameric assembly, human hemoglobin (hHb), in the gas phase. To our knowledge, this is the first report combining ECD and ion-mobility data on the same target protein assembly to delineate the effects of collisional activation on both assembly size and the extent and location of fragmentation. Although the collision-induced unfolding of the hemoglobin assembly is clearly seen by both IMMS and ECD, the latter delineates the regions that increasingly unfold as the collision energy is increased. The results are consistent with previous outcomes for homogeneous protein assemblies and reinforce our interpretation that activation opens the structure of the protein assembly from the flexible regions to make available ECD fragmentation, without dissociating the component proteins.

Indexed as

Amino Acid SequenceCrystallography, X-RayHemoglobinsHumansModels, MolecularProtein MultimerizationProtein Structure, SecondarySpectrometry, Mass, Electrospray IonizationHemoglobinsB factorelectron capture dissociationhemoglobinion mobilitymass spectrometryprotein assembly

Identifiers

PMID26032343
PMCPMC4534183

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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.