Evidence map›Paper›PMID 17114224›Full record

ArticleBiophysical journal2007

FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein.

Petr V Nazarov, Rob B M Koehorst, Werner L Vos, Vladimir V Apanasovich, Marcus A Hemminga

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Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

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  13. Visualization of protein interactions in living cells.Advances in experimental medicine and biology · 2008
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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

5 authors at 2 institutions in 2 countries.

Petr V NazarovLaboratory of Biophysics, Wageningen University, Wageningen, The Netherlands.
Rob B M Koehorst
Werner L Vos
Vladimir V Apanasovich
Marcus A Hemminga
Wageningen University & Research · NLBelarusian State University · BY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A formalism for membrane protein structure determination was developed. This method is based on steady-state FRET data and information about the position of the fluorescence maxima on site-directed fluorescent labeled proteins in combination with global data analysis utilizing simulation-based fitting. The methodology was applied to determine the structural properties of the N-terminal domain of the major coat protein from bacteriophage M13 reconstituted into unilamellar DOPC/DOPG (4:1 mol/mol) vesicles. For our purpose, the cysteine mutants A7C, A9C, N12C, S13C, Q15C, A16C, S17C, and A18C in the N-terminal domain of this protein were produced and specifically labeled with the fluorescence probe AEDANS. The energy transfer data from the natural Trp-26 to AEDANS were analyzed assuming a two-helix protein model. Furthermore, the polarity Stokes shift of the AEDANS fluorescence maxima is taken into account. As a result the orientation and tilt of the N-terminal protein domain with respect to the bilayer interface were obtained, showing for the first time, to our knowledge, an overall alpha-helical protein conformation from amino acid residues 12-46, close to the protein conformation in the intact phage.

Indexed as

Models, BiologicalBacteriophage M13Capsid ProteinsComputer SimulationCysteineFluorescence Resonance Energy TransferFluorescent DyesLipid BilayersMembrane ProteinsMutagenesis, Site-DirectedNaphthalenesulfonatesPhosphatidylcholinesPhosphatidylglycerolsProtein Structure, Tertiary1,2-dioleoyl-sn-glycero-3-phosphoglycerol1,2-oleoylphosphatidylcholine1,5-AEDANSCapsid ProteinsCysteineFluorescent DyesLipid BilayersMembrane ProteinsNaphthalenesulfonatesPhosphatidylcholinesPhosphatidylglycerols

Identifiers

PMID17114224
PMCPMC1783881
OpenAlexW2111359346

What OpenQuestion holds

Textmetadata
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.