pone.0226123.g004.tif (3.96 MB)
Evaluation of rhodopsin (Rh) H1/H8 dimer row structure stability dependence on saturated lipid domain size.
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posted on 2020-02-07, 18:28 authored by Yukito Kaneshige, Fumio Hayashi, Kenichi Morigaki, Yasushi Tanimoto, Hayato Yamashita, Masashi Fujii, Akinori Awazu(a) Averages of 〈S(t)〉t over ten simulations, 〈S(t)〉 where the system consisted of only two H1/H8 dimers and various numbers of saturated and unsaturated lipids (S5 Fig). Error bars indicate standard deviations. 〈S(t)〉t was the average time of S(t) between 50 to 100 μs and was evaluated according to the change in number of saturated lipids between two Rh-dimers. (b) Typical simulation snapshots at time (t) = 50 μs for several different numbers of saturated lipids (Ns = 0–7), where the saturated lipids were placed between parallel two Rh-dimers at t = 0 s (S5 Fig). At time (t) = 50 μs, two Rh dimers are disassembled mostly in the case of Ns = 0 and 1.
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row structureraftophilic regionsparticle populationsdisk membranespalmitoyl moietiesrod-photoreceptor cellsdisk membrane modelRh moleculeform dimerorder structureRh exhibits raftophilicityraftophilic lipidsphototransduction efficiencyphototransduction cascadeG protein-coupled receptorsingle-photon regimedisk membraneform rowsRh-dimer raftophilicityrow structuresdynamics simulationphotopigment protein rhodopsinlipid raftoligomer formationGPCRRh dimersnano-sized lipid raft domains actdynamics simulations
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