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Location of the Substrate Binding Site of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli.Q-Band Electron-Nuclear Double Resonance Reveals Out-of-Plane Hydrogen Bonds Stabilize an Anionic Ubisemiquinone in Cytochrome bo3 from Escherichia coli.Regulation of the primary quinone binding conformation by the H subunit in reaction centers from Rhodobacter sphaeroides.Removal of the H subunit results in enhanced exposure of the semiquinone sites in the LM dimer from Rhodobacter sphaeroides to oxidation by ferricyanide and by O2.X-ray transparent microfluidic chips for high-throughput screening and optimization of in meso membrane protein crystallization.Ultrafast Electron Transfer Kinetics in the LM Dimer of Bacterial Photosynthetic Reaction Center from Rhodobacter sphaeroides.Structure of the alternative complex III in a supercomplex with cytochrome oxidase.The Ubiquinol Binding Site of Cytochrome bo3 from Escherichia coli Accommodates Menaquinone and Stabilizes a Functional MenasemiquinoneSingle-particle cryo-EM studies of transmembrane proteins in SMA copolymer nanodiscsCharacterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation
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description
onderzoeker
@nl
researcher ORCID ID = 0000-0001-6070-5545
@en
name
Chang Sun
@ast
Chang Sun
@en
Chang Sun
@es
Chang Sun
@nl
type
label
Chang Sun
@ast
Chang Sun
@en
Chang Sun
@es
Chang Sun
@nl
prefLabel
Chang Sun
@ast
Chang Sun
@en
Chang Sun
@es
Chang Sun
@nl
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P1153
56972893700
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0000-0001-6070-5545