Evidence map›Paper›PMID 27936328›Full record

ArticleThe journal of physical chemistry letters2017

Segmental Deuteration of α-Synuclein for Neutron Reflectometry on Tethered Bilayers.

Zhiping Jiang, Frank Heinrich, Ryan P McGlinchey, James M Gruschus, Jennifer C Lee

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Raman spectral imaging ofBiophysical chemistry · 2021
    Article
  7. Article
  8. Review
  9. SegmentalAngewandte Chemie (International ed. in English) · 2018
    Article
  10. Article
  11. Article
  12. Propensity for cis-Proline Formation in Unfolded Proteins.Chembiochem : a European journal of chemical biology · 2018
    Article
  13. 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

5 authors.

Zhiping JiangLaboratory of Protein Conformation and Dynamics, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda, Maryland 20892, United States.
Frank HeinrichDepartment of Physics, Carnegie Mellon University , Pittsburgh, Pennsylvania 15213, United States.
Ryan P McGlincheyLaboratory of Protein Conformation and Dynamics, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda, Maryland 20892, United States.
James M GruschusLaboratory of Protein Conformation and Dynamics, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda, Maryland 20892, United States.
Jennifer C LeeLaboratory of Protein Conformation and Dynamics, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda, Maryland 20892, United States.ORCID http://orcid.org/0000-0003-0506-8349

Funding

Protein Misfolding and AggregationZIAHL001055 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEE, JENNIFER · 2009 to 2025
$16.9M
Intramural NIH HHS ZIA HL001055
6 · The paper itself

Abstract

Neutron reflectometry (NR) is uniquely suited for studying protein interaction with phospholipid bilayers along the bilayer normal on an angstrom scale. However, NR on its own cannot discern specific membrane-bound regions due to a lack of scattering contrast within a protein. Here we report the successful coupling of native chemical ligation (NCL) and NR to study α-synuclein (α-syn), a membrane-binding neuronal protein central in Parkinson's disease. Two α-syn variants were generated where either the first 86 or last 54 residues are deuterated, allowing for region-specific contrast within the protein and the identification of membrane interacting residues by NR. Residues 1-86 are positioned at the hydrocarbon/headgroup interface of the outer leaflet, whereas the density distribution of the 54 C-terminal residues ranges from the hydrocarbon region to the aqueous environment. Coupling of NCL and NR should have broad utility in studies of membrane protein folding.

Identifiers

PMID27936328
PMCPMC5367044

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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.