A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Lipid Fingerprints and Cofactor Dynamics of Light-Harvesting Complex II in Different Membranes
Tekijät: Thallmair S, Vainikka PA, Marrink SJ
Kustantaja: CELL PRESS
Julkaisuvuosi: 2019
Journal: Biophysical Journal
Tietokannassa oleva lehden nimi: BIOPHYSICAL JOURNAL
Lehden akronyymi: BIOPHYS J
Vuosikerta: 116
Numero: 8
Aloitussivu: 1446
Lopetussivu: 1455
Sivujen määrä: 10
ISSN: 0006-3495
eISSN: 1542-0086
DOI: https://doi.org/10.1016/j.bpj.2019.03.009
Tiivistelmä
Plant light-harvesting complex II (LHCII) is the key antenna complex for plant photosynthesis. We present coarse-grained molecular dynamics simulations of monomeric and trimeric LHCII in a realistic thylakoid membrane environment based on the Martini force field. The coarse-grained protein model has been optimized with respect to atomistic reference simulations. Our simulations provide detailed insights in the thylakoid lipid fingerprint of LHCII which compares well with experimental data from membrane protein purification. Comparing the monomer and trimeric LHCII reveals a stabilizing effect of trimerization on the chromophores as well as the protein. Moreover, the average chromophore distance shortens in the trimer leading to stronger excitonic couplings. When changing the native thylakoid environment to a model membrane the protein flexibility remains constant, whereas the chromophore flexibility is reduced. Overall, the presented LHCII model lays the foundation to investigate the mu s dynamics of this key antenna protein of plants.
Plant light-harvesting complex II (LHCII) is the key antenna complex for plant photosynthesis. We present coarse-grained molecular dynamics simulations of monomeric and trimeric LHCII in a realistic thylakoid membrane environment based on the Martini force field. The coarse-grained protein model has been optimized with respect to atomistic reference simulations. Our simulations provide detailed insights in the thylakoid lipid fingerprint of LHCII which compares well with experimental data from membrane protein purification. Comparing the monomer and trimeric LHCII reveals a stabilizing effect of trimerization on the chromophores as well as the protein. Moreover, the average chromophore distance shortens in the trimer leading to stronger excitonic couplings. When changing the native thylakoid environment to a model membrane the protein flexibility remains constant, whereas the chromophore flexibility is reduced. Overall, the presented LHCII model lays the foundation to investigate the mu s dynamics of this key antenna protein of plants.
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