Plant LHC-like proteins show robust folding and static non-photochemical quenching.

doi:10.1038/s41467-021-27155-1

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Plant LHC-like proteins show robust folding and static non-photochemical quenching.

Nature communications - 25 Nov 2021

Skotnicová Petra, Staleva-Musto Hristina, Kuznetsova Valentyna, Bína David, Konert Minna M, Lu Shan, Polívka Tomáš, Sobotka Roman

Abstract excerpt

Life on Earth depends on photosynthesis, the conversion of light energy into chemical energy. Plants collect photons by light harvesting complexes (LHC)-abundant membrane proteins containing chlorophyll and xanthophyll molecules. LHC-like proteins are similar in their amino acid sequence to true LHC antennae, however, they rather serve a photoprotective function. Whether the LHC-like proteins bind pigments has...

Topics

Arabidopsis Proteins
Carotenoids
Chlorophyll
Chloroplast Proteins
Energy Transfer
Mutation
Protein Binding
Protein Folding
Protein Multimerization
Synechocystis
Xanthophylls
Zeaxanthins

Source

Open in PubMed Open full text

Identifiers

PMID: 34824207
DOI: 10.1038/s41467-021-27155-1
PMCID: PMC8617258

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics