Evidence map›Paper›PMID 21952771›Full record

ArticleJournal of the American Society for Mass Spectrometry2011

Characterizing the intramolecular H-bond and secondary structure in methylated GlyGlyH+ with H2 predissociation spectroscopy.

Christopher M Leavitt, Arron B Wolk, Michael Z Kamrath, Etienne Garand, Michael J Van Stipdonk, Mark A Johnson

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

6 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
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  5. Article
  6. Infrared Spectroscopy of Mobility-Selected H+-Gly-Pro-Gly-Gly (GPGG).Journal of the American Society for Mass Spectrometry · 2015
    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 3 institutions in 1 country.

Christopher M LeavittSterling Chemistry Laboratory, Yale University, P.O. Box 208107, New Haven, CT 06520, USA.
Arron B Wolk
Michael Z Kamrath
Etienne Garand
Michael J Van Stipdonk
Mark A Johnson
Yale University · USSterling Research Group · USWichita State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report vibrational predissociation spectra of the four protonated dipeptides derived from glycine and sarcosine, GlyGlyH(+)•(H(2))(1,2), GlySarH(+)•(D(2))(2), SarGlyH(+)•(H(2))(2), and SarSarH(+)•(D(2))(2), generated in a cryogenic ion trap. Sharp bands were recovered by monitoring photoevaporation of the weakly bound H(2) (D(2)) molecules in a linear action regime throughout the 700-4200 cm(-1) range using a table-top laser system. The spectral patterns were analyzed in the context of the low energy structures obtained from electronic structure calculations. These results indicate that all four species are protonated on the N-terminus, and feature an intramolecular H-bond involving the amino group. The large blue-shift in the H-bonded N-H fundamental upon incorporation of a methyl group at the N-terminus indicates that this modification significantly lowers the strength of the intramolecular H-bond. Methylation at the amide nitrogen, on the other hand, induces a significant rotation (~110°) about the peptide backbone.

Indexed as

DipeptidesGlycylglycineHydrogen BondingMethylationPhotochemical ProcessesProtein Structure, SecondaryProtonsSpectrometry, Mass, Electrospray IonizationSpectrophotometry, InfraredVibrationDipeptidesGlycylglycineglycylsarcosineProtons

Identifiers

PMID21952771
OpenAlexW2041379151

What OpenQuestion holds

Textmetadata
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.