ArticleBiophysical chemistry2011
Interaction of a two-transmembrane-helix peptide with lipid bilayers and dodecyl sulfate micelles.
Article in Biophysical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Deep learning reveals antibiotics in the archaeal proteome.Nature microbiology · 2025Article
- Computational exploration of global venoms for antimicrobial discovery with Venomics artificial intelligence.Nature communications · 2025Article
- Discovery of antibiotics in the archaeome using deep learning.bioRxiv : the preprint server for biology · 2024Article
- New linear antiplasmodial peptides related to angiotensin II.Malaria journal · 2015Article
- Fluorophores, environments, and quantification techniques in the analysis of transmembrane helix interaction using FRET.Biopolymers · 2015Review
- Fluorescence spectroscopy of rhodopsins: insights and approaches.Biochimica et biophysica acta · 2014Review
- The transmembrane domains of the bacterial cell division proteins FtsB and FtsL form a stable high-order oligomer.Biochemistry · 2013Article
- Detergent-mediated protein aggregation.Chemistry and physics of lipids · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
To probe structural changes that occur when a membrane protein is transferred from lipid bilayers to SDS micelles, a fragment of bacteriorhodopsin containing transmembrane helical segments A and B was studied by fluorescence spectroscopy, molecular dynamics (MD) simulation, and stopped flow kinetics. In lipid bilayers, Förster resonance energy transfer (FRET) was observed between tyrosine 57 on helix B and tryptophans 10 and 12 on helix A. FRET efficiency decreased substantially when the peptide was transferred to SDS. MD simulation showed no evidence for significant disruption of helix-helix interactions in SDS micelles. However, a cluster of water molecules was observed to form a hydrogen-bonded network with the phenolic hydroxyl group of tyrosine 57, which probably causes the disappearance of tyrosine-to-tryptophan FRET in SDS. The tryptophan quantum yield decreased in SDS, and the change occurred at nearly the same rate as membrane solubilization. The results provide a clear example of the importance of corroborating distance changes inferred from FRET by using complementary methods.
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Registered trials
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.