Evidence map›Paper›PMID 18761457›Full record

ArticleJournal of the American Chemical Society2008

Electron capture by a hydrated gaseous peptide: effects of water on fragmentation and molecular survival.

James S Prell, Jeremy T O'Brien, Anne I S Holm, Ryan D Leib, William A Donald, Evan R Williams

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. 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
3.1field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Low-Energy Electron Damage to Condensed-Phase DNA and Its Constituents.International journal of molecular sciences · 2021
    Review
  3. Probing Protein Structure and Folding in the Gas Phase by Electron Capture Dissociation.Journal of the American Society for Mass Spectrometry · 2015
    Article
  4. Article
  5. Electron capture dissociation of trivalent metal ion-peptide complexes.Journal of the American Society for Mass Spectrometry · 2013
    Article
  6. Article
  7. Article
  8. Article
  9. Gas-phase chemistry of multiply charged bioions in analytical mass spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2010
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

6 authors at 1 institution in 1 country.

James S PrellDepartment of Chemistry, University of California, Berkeley, California 94720-1460, USA.
Jeremy T O'Brien
Anne I S Holm
Ryan D Leib
William A Donald
Evan R Williams
University of California, Berkeley · US

Funding

Protein Conformation and Noncovalent InteractionsR01GM064712 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2002 to 2009
$2.0M
NIGMS NIH HHS R01 GM064712NIGMS NIH HHS R01GM064712
6 · The paper itself

Abstract

The effects of water on electron capture dissociation products, molecular survival, and recombination energy are investigated for diprotonated Lys-Tyr-Lys solvated by between zero and 25 water molecules. For peptide ions with between 12 and 25 water molecules attached, electron capture results in a narrow distribution of product ions corresponding to primarily the loss of 10-12 water molecules from the reduced precursor. From these data, the recombination energy (RE) is determined to be equal to the energy that is lost by evaporating on average 10.7 water molecules, or 4.3 eV. Because water stabilizes ions, this value is a lower limit to the RE of the unsolvated ion, but it indicates that the majority of the available RE is deposited into internal modes of the peptide ion. Plotting the fragment ion abundances for ions formed from precursors with fewer than 11 water molecules as a function of hydration extent results in an energy resolved breakdown curve from which the appearance energies of the b 2 (+), y 2 (+), z 2 (+*), c 2 (+), and (KYK + H) (+) fragment ions formed from this peptide ion can be obtained; these values are 78, 88, 42, 11, and 9 kcal/mol, respectively. The propensity for H atom loss and ammonia loss from the precursor changes dramatically with the extent of hydration, and this change in reactivity can be directly attributed to a "caging" effect by the water molecules. These are the first experimental measurements of the RE and appearance energies of fragment ions due to electron capture dissociation of a multiply charged peptide. This novel ion nanocalorimetry technique can be applied more generally to other exothermic reactions that are not readily accessible to investigation by more conventional thermochemical methods.

Indexed as

CalorimetryElectronsGasesNanotechnologyOligopeptidesSpectrometry, Mass, Electrospray IonizationThermodynamicsWaterGaseslysyl-tyrosyl-lysineOligopeptidesWater

Identifiers

PMID18761457
PMCPMC2673717
OpenAlexW1997219852

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.