Evidence map›Paper›PMID 11509381›Full record

ArticleBiophysical journal2001

Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance.

M Bak, R P Bywater, M Hohwy, J K Thomsen, K Adelhorst, H J Jakobsen, O W Sørensen, N C Nielsen

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

42 citing papers in PubMed, 112 citations in OpenAlex.

  1. Membrane Topology and Oligomerization of Peptaibols by Solid-State NMR Spectroscopy.Journal of peptide science : an official publication of the European Peptide Society · 2026
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  11. A thermodynamic approach to alamethicin pore formation.Biochimica et biophysica acta · 2014
    Article
  12. Article
  13. Dependence of Alamethicin Membrane Orientation on the Solution Concentration.The journal of physical chemistry. C, Nanomaterials and interfaces · 2013
    Article
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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

8 authors at 3 institutions in 1 country.

M BakLaboratory for Biomolecular NMR Spectroscopy, Department of Molecular and Structural Biology, Science Park, University of Aarhus, DK-8000 Aarhus C, Denmark.
R P Bywater
M Hohwy
J K Thomsen
K Adelhorst
H J Jakobsen
O W Sørensen
N C Nielsen
Aarhus University · DKNovo Nordisk (Denmark) · DKCarlsberg Laboratory · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conformation of the 20-residue antibiotic ionophore alamethicin in macroscopically oriented phospholipid bilayers has been studied using (15)N solid-state nuclear magnetic resonance (NMR) spectroscopy in combination with molecular modeling and molecular dynamics simulations. Differently (15)N-labeled variants of alamethicin and an analog with three of the alpha-amino-isobutyric acid residues replaced by alanines have been investigated to establish experimental structural constraints and determine the orientation of alamethicin in hydrated phospholipid (dimyristoylphosphatidylcholine) bilayers and to investigate the potential for a major kink in the region of the central Pro(14) residue. From the anisotropic (15)N chemical shifts and (1)H-(15)N dipolar couplings determined for alamethicin with (15)N-labeling on the Ala(6), Val(9), and Val(15) residues and incorporated into phospholipid bilayer with a peptide:lipid molar ratio of 1:8, we deduce that alamethicin has a largely linear alpha-helical structure spanning the membrane with the molecular axis tilted by 10-20 degrees relative to the bilayer normal. In particular, we find compatibility with a straight alpha-helix tilted by 17 degrees and a slightly kinked molecular dynamics structure tilted by 11 degrees relative to the bilayer normal. In contrast, the structural constraints derived by solid-state NMR appear not to be compatible with any of several model structures crossing the membrane with vanishing tilt angle or the earlier reported x-ray diffraction structure (Fox and Richards, Nature. 300:325-330, 1982). The solid-state NMR-compatible structures may support the formation of a left-handed and parallel multimeric ion channel.

Indexed as

AlamethicinLipid BilayersModels, MolecularNuclear Magnetic Resonance, BiomolecularPhospholipidsProtein ConformationAlamethicinLipid BilayersPhospholipids

Identifiers

PMID11509381
PMCPMC1301646
OpenAlexW2065660960

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.