Evidence map›Paper›PMID 25360896›Full record

ArticleThe journal of physical chemistry. B2014

Distance geometry protocol to generate conformations of natural products to structurally interpret ion mobility-mass spectrometry collision cross sections.

Sarah M Stow, Cody R Goodwin, Michal Kliman, Brian O Bachmann, John A McLean, Terry P Lybrand

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

3 citing papers in PubMed.

  1. Article
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  3. Review
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.

Sarah M StowDepartment of Chemistry, ‡Department of Pharmacology, §Vanderbilt Institute of Chemical Biology, ∥Vanderbilt Institute of Integrative Biosystems Research and Education, ⊥Center for Structural Biology, Vanderbilt University , Nashville, Tennessee 37235, United States.
Cody R Goodwin
Michal Kliman
Brian O Bachmann
John A McLean
Terry P Lybrand

Funding

New Methodologies for Accelerating Natural Product DiscoveryR01GM092218 · NIGMS · VANDERBILT UNIVERSITY · PI BACHMANN, BRIAN O, MCLEAN, JOHN ALAN · 2010 to 2018
$2.8M
NIGMS NIH HHS R01 GM092218NIGMS NIH HHS R01GM092218
6 · The paper itself

Abstract

Ion mobility-mass spectrometry (IM-MS) allows the separation of ionized molecules based on their charge-to-surface area (IM) and mass-to-charge ratio (MS), respectively. The IM drift time data that is obtained is used to calculate the ion-neutral collision cross section (CCS) of the ionized molecule with the neutral drift gas, which is directly related to the ion conformation and hence molecular size and shape. Studying the conformational landscape of these ionized molecules computationally provides interpretation to delineate the potential structures that these CCS values could represent, or conversely, structural motifs not consistent with the IM data. A challenge in the IM-MS community is the ability to rapidly compute conformations to interpret natural product data, a class of molecules exhibiting a broad range of biological activity. The diversity of biological activity is, in part, related to the unique structural characteristics often observed for natural products. Contemporary approaches to structurally interpret IM-MS data for peptides and proteins typically utilize molecular dynamics (MD) simulations to sample conformational space. However, MD calculations are computationally expensive, they require a force field that accurately describes the molecule of interest, and there is no simple metric that indicates when sufficient conformational sampling has been achieved. Distance geometry is a computationally inexpensive approach that creates conformations based on sampling different pairwise distances between the atoms within the molecule and therefore does not require a force field. Progressively larger distance bounds can be used in distance geometry calculations, providing in principle a strategy to assess when all plausible conformations have been sampled. Our results suggest that distance geometry is a computationally efficient and potentially superior strategy for conformational analysis of natural products to interpret gas-phase CCS data.

Indexed as

Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationBiological ProductsGasesIonsMolecular ConformationMolecular Dynamics SimulationPeptidesProteinsBiological ProductsGasesIonsPeptidesProteins

Identifiers

PMID25360896
PMCPMC4259499

What OpenQuestion holds

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Registered trials

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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.