Evidence map›Paper›PMID 28211014›Full record

ArticleJournal of the American Society for Mass Spectrometry2017

Comprehensive Peptide Ion Structure Studies Using Ion Mobility Techniques: Part 1. An Advanced Protocol for Molecular Dynamics Simulations and Collision Cross-Section Calculation.

Samaneh Ghassabi Kondalaji, Mahdiar Khakinejad, Amirmahdi Tafreshian, Stephen J Valentine

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. 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

4 authors.

Samaneh Ghassabi KondalajiC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, WV, 26506, USA.
Mahdiar KhakinejadC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, WV, 26506, USA.
Amirmahdi TafreshianDepartment of Statistics, West Virginia University, P.O. Box 6330, Morgantown, WV, 26506, USA.
Stephen J ValentineC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, WV, 26506, USA. stephen.valentine@mail.wvu.edu.ORCID 0000-0003-4360-2928

Funding

Developing IMS-SID/MAD-MS Instrumentation for Characterizing Intrinsically Disordered Protein StructureR01GM114494 · NIGMS · WEST VIRGINIA UNIVERSITY · PI VALENTINE, STEPHEN · 2015 to 2019
$1.4M
NIGMS NIH HHS R01 GM114494
6 · The paper itself

Abstract

Collision cross-section (CCS) measurements with a linear drift tube have been utilized to study the gas-phase conformers of a model peptide (acetyl-PAAAAKAAAAKAAAAKAAAAK). Extensive molecular dynamics (MD) simulations have been conducted to derive an advanced protocol for the generation of a comprehensive pool of in-silico structures; both higher energy and more thermodynamically stable structures are included to provide an unbiased sampling of conformational space. MD simulations at 300 K are applied to the in-silico structures to more accurately describe the gas-phase transport properties of the ion conformers including their dynamics. Different methods used previously for trajectory method (TM) CCS calculation employing the Mobcal software [1] are evaluated. A new method for accurate CCS calculation is proposed based on clustering and data mining techniques. CCS values are calculated for all in-silico structures, and those with matching CCS values are chosen as candidate structures. With this approach, more than 300 candidate structures with significant structural variation are produced; although no final gas-phase structure is proposed here, in a second installment of this work, gas-phase hydrogen deuterium exchange data will be utilized as a second criterion to select among these structures as well as to propose relative populations for these ion conformers. Here the need to increase conformer diversity and accurate CCS calculation is demonstrated and the advanced methods are discussed. Graphical Abstract ᅟ.

Indexed as

Molecular Dynamics SimulationAlgorithmsAmino Acid SequenceGasesIonsMass SpectrometryPeptidesProtein Structure, SecondaryGasesIonsPeptidesCluster analysisCollision cross-section calculationConformational space samplingIon mobility spectrometry

Identifiers

PMID28211014
PMCPMC5942881

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.