A1 Refereed original research article in a scientific journal
Lipid Fingerprints and Cofactor Dynamics of Light-Harvesting Complex II in Different Membranes
Authors: Thallmair S, Vainikka PA, Marrink SJ
Publisher: CELL PRESS
Publication year: 2019
Journal: Biophysical Journal
Journal name in source: BIOPHYSICAL JOURNAL
Journal acronym: BIOPHYS J
Volume: 116
Issue: 8
First page : 1446
Last page: 1455
Number of pages: 10
ISSN: 0006-3495
eISSN: 1542-0086
DOI: https://doi.org/10.1016/j.bpj.2019.03.009
Abstract
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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