Evidence map›Paper›PMID 27747952›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2017

Optimal Bicelle Size q for Solution NMR Studies of the Protein Transmembrane Partition.

Alessandro Piai, Qingshan Fu, Jyoti Dev, James J Chou

Open access · greenAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 53 citations in OpenAlex.

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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 at 1 institution in 1 country.

Alessandro PiaiDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, 02115, USA.ORCID http://orcid.org/0000-0002-5264-1980
Qingshan FuDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, 02115, USA.
Jyoti DevDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, 02115, USA.
James J ChouDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, 02115, USA.
Harvard University · US

Funding

Structures of Alpha 4 Integrins, Ligands and AntagonistsP01HL103526 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 2011 to 2015
$11.1M
Function and mechanism of the HCV p7 channel and its therapeutic potentialR01GM116898 · NIGMS · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2016 to 2019
$1.9M
NHLBI NIH HHS P01 HL103526NIGMS NIH HHS R01 GM116898
6 · The paper itself

Abstract

Structural characterization of transmembrane proteins in isotropic bicelles has become an increasingly popular application of solution NMR spectroscopy, as the fast-tumbling bicelles are membrane-like, yet can often yield spectral quality comparable to those of detergent micelles. While larger bicelles are closer to the true lipid bilayer, it remains unclear how large the bicelles need to be to allow accurate assessment of the protein transmembrane partition in the lipid bilayer. Here, we address the above question from the perspective of the protein residing in the bicelles, through systematic measurement of the protein chemical shift and transmembrane partition at different lipid/detergent ratios (q), ranging from 0.3 to 0.7, using the transmembrane domain of the human Fas receptor as model system. We found that the lipid environment of the bicelles, as reflected by the protein chemical shift, begins to be perturbed when q is reduced to below 0.6. We also implemented a solvent paramagnetic relaxation enhancement (PRE) approach for bicelles to show that the protein transmembrane partition in bicelles with q=0.5 and 0.7 are very similar, but at q=0.3 the solvent PRE profile is significantly different. Our data indicate that q values between 0.5 and 0.6 are a good compromise between high resolution NMR and closeness to the membrane environment, and allow accurate characterization of the protein position in the lipid bilayer.

Indexed as

Magnetic Resonance SpectroscopyDimyristoylphosphatidylcholinefas ReceptorHeterocyclic CompoundsHumansLipid BilayersOrganometallic CompoundsPhospholipid EthersRecombinant Proteins1,2-dihexadecyl-sn-glycero-3-phosphocholineDimyristoylphosphatidylcholinefas Receptorgadolinium 1,4,7,10-tetraazacyclododecane-N,N',N'',N'''-tetraacetateHeterocyclic CompoundsLipid BilayersOrganometallic CompoundsPhospholipid EthersRecombinant Proteinsbicellesmembrane proteinsNMR spectroscopyparamagnetic relaxation enhancementtransmembrane partition

Identifiers

PMID27747952
PMCPMC5272838
OpenAlexW2532161328

What OpenQuestion holds

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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.