Evidence map›Paper›PMID 33169002›Full record

ArticleNature protocols2020

Protein higher-order-structure determination by fast photochemical oxidation of proteins and mass spectrometry analysis.

Xiaoran Roger Liu, Don L Rempel, Michael L Gross

Abstract read
In one paragraph

Article in Nature protocols, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

3 authors.

Xiaoran Roger LiuDepartment of Chemistry, Washington University in St. Louis, St. Louis, MO, USA. xliu167@wustl.edu.ORCID http://orcid.org/0000-0003-3198-1588
Don L RempelDepartment of Chemistry, Washington University in St. Louis, St. Louis, MO, USA.
Michael L GrossDepartment of Chemistry, Washington University in St. Louis, St. Louis, MO, USA. mgross@wustl.edu.ORCID http://orcid.org/0000-0003-1159-4636

Funding

TrainingP41GM103422 · NIGMS · WASHINGTON UNIVERSITY · PI YARASHESKI, KEVIN E · 2012 to 2019
$12.0M
A Biomedical Mass Spectrometry Resource: Ongoing Driving Biomedical ProjectsR24GM136766 · NIGMS · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 2020 to 2022
$2.3M
A MASS SPECTROMETER FOR PROTEIN FOOTPRINTINGS10OD016298 · OD · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 2014 to 2014
$450k
Mechano sensitive peptide aggregates for targeted therapyR15GM135766 · NIGMS · UNIVERSITY OF MICHIGAN AT DEARBORN · PI KANAPATHIPILLAI, MATHUMAI · 2020 to 2020
$443k
NIGMS NIH HHS P41 GM103422NIGMS NIH HHS R15 GM135766NIGMS NIH HHS R24 GM136766NIH HHS S10 OD016298
6 · The paper itself

Abstract

The higher-order structure (HOS) of proteins plays a critical role in their function; therefore, it is important to our understanding of their function that we have as much information as possible about their three-dimensional structure and how it changes with time. Mass spectrometry (MS) has become an important tool for determining protein HOS owing to its high throughput, mid-to-high spatial resolution, low sample amount requirement and broad compatibility with various protein systems. Modern MS-based protein HOS analysis relies, in part, on footprinting, where a reagent reacts 'to mark' the solvent-accessible surface of the protein, and MS-enabled proteomic analysis locates the modifications to afford a footprint. Fast photochemical oxidation of proteins (FPOP), first introduced in 2005, has become a powerful approach for protein footprinting. Laser-induced hydrogen peroxide photolysis generates hydroxyl radicals that react with solvent-accessible side chains (14 out of 20 amino acid side chains) to fulfill the footprinting. The reaction takes place at sub-milliseconds, faster than most of labeling-induced protein conformational changes, thus enabling a 'snapshot' of protein HOS in solution. As a result, FPOP has been employed in solving several important problems, including mapping epitopes, following protein aggregation, locating small molecule binding, measuring ligand-binding affinity, monitoring protein folding and unfolding and determining hidden conformational changes invisible to other methods. Broader adoption will be promoted by dissemination of the technical details for assembling the FPOP platform and for dealing with the complexities of analyzing FPOP data. In this protocol, we describe the FPOP platform, the conditions for successful footprinting and its examination by mass measurements of the intact protein, the post-labeling sample handling and digestion, the liquid chromatography-tandem MS analysis of the digested sample and the data analysis with Protein Metrics Suite. This protocol is intended not only as a guide for investigators trying to establish an FPOP platform in their own lab but also for those willing to incorporate FPOP as an additional tool in addressing their questions of interest.

Indexed as

Photochemical ProcessesKineticsMass SpectrometryModels, MolecularOxidation-ReductionProtein ConformationProteinsProteins

Identifiers

PMID33169002
PMCPMC10476649

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.