Evidence map›Paper›PMID 21943415›Full record

ArticleBiophysical journal2011

Time-resolved WAXS reveals accelerated conformational changes in iodoretinal-substituted proteorhodopsin.

Erik Malmerberg, Ziad Omran, Jochen S Hub, Xuewen Li, Gergely Katona, Sebastian Westenhoff, Linda C Johansson, Magnus Andersson, Marco Cammarata, Michael Wulff and 4 more

Abstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

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

35 citing papers in PubMed.

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  12. Tracking Membrane Protein Dynamics in Real Time.The Journal of membrane biology · 2021
    Review
  13. Article
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  15. Tracking CaScience advances · 2020
    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

14 authors.

Erik MalmerbergDepartment of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Gothenburg, Sweden.
Ziad Omran
Jochen S Hub
Xuewen Li
Gergely Katona
Sebastian Westenhoff
Linda C Johansson
Magnus Andersson
Marco Cammarata
Michael Wulff
David van der Spoel
Jan Davidsson
Alexandre Specht
Richard Neutze

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Time-resolved wide-angle x-ray scattering (TR-WAXS) is an emerging biophysical method which probes protein conformational changes with time. Here we present a comparative TR-WAXS study of native green-absorbing proteorhodopsin (pR) from SAR86 and a halogenated derivative for which the retinal chromophore has been replaced with 13-desmethyl-13-iodoretinal (13-I-pR). Transient absorption spectroscopy differences show that the 13-I-pR photocycle is both accelerated and displays more complex kinetics than native pR. TR-WAXS difference data also reveal that protein structural changes rise and decay an order-of-magnitude more rapidly for 13-I-pR than native pR. Despite these differences, the amplitude and nature of the observed helical motions are not significantly affected by the substitution of the retinal's C-20 methyl group with an iodine atom. Molecular dynamics simulations indicate that a significant increase in free energy is associated with the 13-cis conformation of 13-I-pR, consistent with our observation that the transient 13-I-pR conformational state is reached more rapidly. We conclude that although the conformational trajectory is accelerated, the major transient conformation of pR is unaffected by the substitution of an iodinated retinal chromophore.

Indexed as

X-Ray DiffractionColorIodineIsomerismModels, MolecularProtein ConformationRetinaldehydeRhodopsinRhodopsins, MicrobialThermodynamicsTime FactorsIodineproteorhodopsinRetinaldehydeRhodopsinRhodopsins, Microbial

Identifiers

PMID21943415
PMCPMC3177065

What OpenQuestion holds

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Registered trials

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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.