Evidence map›Paper›PMID 41521558›Full record

ArticleBiophysical journal2026

Time-resolved x-ray solution scattering from detergent solubilized visual rhodopsin.

Daniel Sarabi, Lucija Ostojić, Xiaolin Xu, Thomas Gruhl, Niranjan Varma, Robert Bosman, Oskar Berntsson, Martin Nors Pedersen, Mathias Sander, Michael Wulff and 5 more

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Article in Biophysical journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

15 authors.

Daniel SarabiDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Lucija OstojićDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Xiaolin XuDepartment of Physics, University of Arizona, Tucson, Arizona.
Thomas GruhlDivision of Biology and Chemistry, Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen PSI, Switzerland.
Niranjan VarmaDivision of Biology and Chemistry, Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen PSI, Switzerland.
Robert BosmanDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Oskar BerntssonDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Martin Nors PedersenESRF - The European Synchrotron, Grenoble, France.
Mathias SanderESRF - The European Synchrotron, Grenoble, France.
Michael WulffESRF - The European Synchrotron, Grenoble, France.
Matteo LevantinoESRF - The European Synchrotron, Grenoble, France.
Gebhard F X SchertlerDivision of Biology and Chemistry, Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen PSI, Switzerland.
Michael F BrownDepartment of Physics, University of Arizona, Tucson, Arizona; Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona.
Valerie PanneelsDivision of Biology and Chemistry, Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen PSI, Switzerland.
Richard NeutzeDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden. Electronic address: richard.neutze@chem.gu.se.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Time-resolved x-ray solution scattering (TR-XSS) studies provide experimental probes of transient conformational states in macromolecules. Difference x-ray scattering curves from integral membrane proteins are predicted to be influenced by the presence of the surrounding detergent micelle. Here, we present time-dependent x-ray solution scattering data from visual rhodopsin when solubilized in two different detergents: the nonionic surfactant n-dodecyl-β-D-maltoside and the zwitterionic detergent 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate. Both detergents produce micelles that surround rhodopsin, yet they have different composition, density and critical micelle concentrations and yield different x-ray scattering properties. Our theoretical framework is able to fit the experimental TR-XSS data for photoactivated rhodopsin in both detergents, yielding experimental verification of how x-ray scattering contrast from the detergent molecules influences difference x-ray scattering measurements from integral membrane proteins. These results increase confidence when modeling conformational changes of integral membrane proteins from an ensemble of predicted structures.

Indexed as

DetergentsRhodopsinScattering, RadiationX-Ray DiffractionAnimalsCholic AcidsGlucosidesMicellesSolubilitySolutionsTime Factors3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonateCholic AcidsDetergentsdodecyl maltosideGlucosidesMicellesRhodopsinSolutions

Identifiers

PMID41521558
PMCPMC13351589

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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.