Evidence map›Paper›PMID 19843458›Full record

ArticleBiophysical journal2009

Tilt and rotation angles of a transmembrane model peptide as studied by fluorescence spectroscopy.

Andrea Holt, Rob B M Koehorst, Tania Rutters-Meijneke, Michael H Gelb, Dirk T S Rijkers, Marcus A Hemminga, J Antoinette Killian

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 54 citations in OpenAlex.

  1. Hydrophobic mismatch induces lipid sorting based on tail unsaturation.bioRxiv : the preprint server for biology · 2026
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  7. Diverse Scientific Benchmarks for Implicit Membrane Energy Functions.Journal of chemical theory and computation · 2021
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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

7 authors at 3 institutions in 2 countries.

Andrea HoltChemical Biology and Organic Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands. a.holt@nki.nl
Rob B M Koehorst
Tania Rutters-Meijneke
Michael H Gelb
Dirk T S Rijkers
Marcus A Hemminga
J Antoinette Killian
Utrecht University · NLWageningen University & Research · NLUniversity of Washington · US

Funding

Electron Paramagnetic Resonance (EPR)/Q-Band ENDOR SpectrometerS10RR023065 · NCRR · UNIVERSITY OF WASHINGTON · PI ROBINSON, BRUCE H · 2007 to 2007
$1.0M
NCRR NIH HHS 1S10RR023065-01NCRR NIH HHS S10 RR023065
6 · The paper itself

Abstract

In this study the membrane orientation of a tryptophan-flanked model peptide, WALP23, was determined by using peptides that were labeled at different positions along the sequence with the environmentally sensitive fluorescent label BADAN. The fluorescence properties, reflecting the local polarity, were used to determine the tilt and rotation angles of the peptide based on an ideal alpha-helix model. For WALP23 inserted in dioleoylphosphatidylcholine (DOPC), an estimated tilt angle of the helix with respect to the bilayer normal of 24 degrees +/- 5 degrees was obtained. When the peptides were inserted into bilayers with different acyl chain lengths or containing different concentrations of cholesterol, small changes in tilt angle were observed as response to hydrophobic mismatch, whereas the rotation angle appeared to be independent of lipid composition. In all cases, the tilt angles were significantly larger than those previously determined from (2)H NMR experiments, supporting recent suggestions that the relatively long timescale of (2)H NMR measurements may result in an underestimation of tilt angles due to partial motional averaging. It is concluded that although the fluorescence technique has a rather low resolution and limited accuracy, it can be used to resolve the discrepancies observed between previous (2)H NMR experiments and molecular-dynamics simulations.

Indexed as

Models, Chemical2-NaphthylamineCholesterolFluorescenceHydrophobic and Hydrophilic InteractionsLipid BilayersPeptidesPhosphatidylcholinesProtein Structure, SecondaryRotationSpectrometry, Fluorescence1,2-oleoylphosphatidylcholine2-Naphthylamine6-bromoacetyl-2-dimethylaminonaphthaleneCholesterolLipid BilayersPeptidesPhosphatidylcholines

Identifiers

PMID19843458
PMCPMC2764067
OpenAlexW2000436622

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.