Evidence map›Paper›PMID 33285116›Full record

ArticleBiophysical journal2021

Conformational Dynamics of Light-Harvesting Complex II in a Native Membrane Environment.

Fatemeh Azadi-Chegeni, Meaghan E Ward, Giorgio Perin, Diana Simionato, Tomas Morosinotto, Marc Baldus, Anjali Pandit

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

8 citing papers in PubMed, 22 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2025
    Article
  2. Conformational Dynamics of BacteriochlorophyllThe journal of physical chemistry. B · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. 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

7 authors at 3 institutions in 2 countries.

Fatemeh Azadi-ChegeniDepartment of Solid-state NMR, Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, Leiden, the Netherlands.
Meaghan E WardDepartment of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, the Netherlands.
Giorgio PerinPAR-Lab (Padua Algae Research Laboratory), Department of Biology, University of Padua, Padua, Italy.
Diana SimionatoPAR-Lab (Padua Algae Research Laboratory), Department of Biology, University of Padua, Padua, Italy.
Tomas MorosinottoPAR-Lab (Padua Algae Research Laboratory), Department of Biology, University of Padua, Padua, Italy.
Marc BaldusDepartment of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, the Netherlands.
Anjali PanditDepartment of Solid-state NMR, Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, Leiden, the Netherlands. Electronic address: a.pandit@chem.leidenuniv.nl.
University of Padua · ITLeiden University · NLUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic light-harvesting complexes (LHCs) of higher plants, moss, and green algae can undergo dynamic conformational transitions, which have been correlated to their ability to adapt to fluctuations in the light environment. Herein, we demonstrate the application of solid-state NMR spectroscopy on native, heterogeneous thylakoid membranes of Chlamydomonas reinhardtii (Cr) and on Cr light-harvesting complex II (LHCII) in thylakoid lipid bilayers to detect LHCII conformational dynamics in its native membrane environment. We show that membrane-reconstituted LHCII contains selective sites that undergo fast, large-amplitude motions, including the phytol tails of two chlorophylls. Protein plasticity is also observed in the N-terminal stromal loop and in protein fragments facing the lumen, involving sites that stabilize the xanthophyll-cycle carotenoid violaxanthin and the two luteins. The results report on the intrinsic flexibility of LHCII pigment-protein complexes in a membrane environment, revealing putative sites for conformational switching. In thylakoid membranes, fast dynamics of protein and pigment sites is significantly reduced, which suggests that in their native organelle membranes, LHCII complexes are locked in specific conformational states.

Indexed as

Chlamydomonas reinhardtiiThylakoidsChlorophyllLight-Harvesting Protein ComplexesPhotosynthesisPhotosystem II Protein ComplexChlorophyllLight-Harvesting Protein ComplexesPhotosystem II Protein Complex

Identifiers

PMID33285116
PMCPMC7840412
OpenAlexW3109394471

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.