about
Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering.Ultrafast structural dynamics of the photocleavage of protein hybrid nanoparticles.Conformational changes of non-B DNA.Reversible conformational switching of i-motif DNA studied by fluorescence spectroscopy.Role of water in directing diphenylalanine assembly into nanotubes and nanowires.Efficient electron transfer in i-motif DNA with a tetraplex structure.Photocycle of Photoactive Yellow Protein in Cell-Mimetic Environments: Molecular Volume Changes and Kinetics.Protein structural dynamics of photoactive yellow protein in solution revealed by pump-probe X-ray solution scattering.Proton Transfer of Guanine Radical Cations Studied by Time-Resolved Resonance Raman Spectroscopy Combined with Pulse Radiolysis.Correction to "Photocycle of Photoactive Yellow Protein in Cell-Mimetic Environments: Molecular Volume Changes and Kinetics".Interaction of G-quadruplex with RecA protein studied in bulk phase and at the single-molecule level.Hole trapping of G-quartets in a G-quadruplex.Detection of Structural Changes upon One-Electron Oxidation and Reduction of Stilbene Derivatives by Time-Resolved Resonance Raman Spectroscopy during Pulse Radiolysis and Theoretical Calculations.Structural study of various substituted biphenyls and their radical anions based on time-resolved resonance Raman spectroscopy combined with pulse radiolysisConfigurational changes of heme followed by cytochrome c folding reactionDynamics in the heme geometry of myoglobin induced by the one-electron reductionRadical cation of star-shaped condensed oligofluorenes having isotruxene as a core: importance of rigid planar structure on charge delocalizationInfluence of Charge Distribution on Structural Changes of Aromatic Imide Derivatives upon One-Electron Reduction Revealed by Time-Resolved Resonance Raman Spectroscopy during Pulse RadiolysisEnhanced photocatalytic activity in composites of TiO2 nanotubes and CdS nanoparticlesFolding dynamics of ferrocytochrome C in a denaturant-free environment probed by transient grating spectroscopyFabrication of silica-coated magnetic nanoparticles with highly photoluminescent lanthanide probesPhotophysical properties of Zn-substituted cytochrome c investigated by single-molecule and ensemble-averaged spectroscopySelf-assembly of polydeoxyadenylic acid studied at the single-molecule levelUnfolding dynamics of cytochrome c revealed by single-molecule and ensemble-averaged spectroscopyProtein folding dynamics of cytochrome c seen by transient grating and transient absorption spectroscopiesFolding dynamics of cytochrome c using pulse radiolysispH-induced intramolecular folding dynamics of i-motif DNAThe time scale of the quaternary structural changes in hemoglobin revealed using the transient grating techniqueStructural Dynamics of Bismuth Triiodide in Solution Triggered by Photoinduced Ligand-to-Metal Charge TransferFormation of the Charge-Localized Dimer Radical Cation of 2-Ethyl-9,10-dimethoxyanthracene in Solution PhaseProton Transfer Accompanied by the Oxidation of AdenosineProtein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering
P50
Q33370898-0021F2EF-35D0-410D-BEEC-A6CADC5446B4Q33876751-F81744AD-06DE-4BCE-9427-9DB0F0C4095FQ37928936-C6120197-0047-4CF7-B83B-268236B3F49CQ38073293-85F9730A-1156-4755-ACDC-D460B9F6AF58Q43135939-2A025F88-B2F5-4EFD-B9D3-6DCD95AF3551Q45195952-C544CF4B-3188-4A2D-9924-0E55FE8687C2Q46436384-E35F09B8-DE9F-4B61-A5DD-CB6C7F160A3FQ46496101-D69AAEA7-0EBD-401E-832D-2FBB99BD258AQ46628780-9AA1536F-6E85-44A0-A1BF-D872D3BC5DB2Q48131533-C0FADABF-FCE0-415B-B738-3D3E1E0D5F92Q51004469-A69FFA19-BCB5-4233-AA7D-925730E73D71Q53351903-227DE177-F705-4BE2-A91E-EEE4FE0AEEA2Q53474928-7633E2B9-BEA2-4BF5-9069-B93AE92F90CAQ57160945-85D804F1-C2D6-45A9-A22E-CE1E341966F8Q57161622-DECF28EB-7A37-4973-BDFC-8E3F881CFC12Q57163909-19C479EA-83D8-469A-BDA6-742D5713EBA1Q57164471-FDE57011-3972-4D07-B81D-1ADE7F904491Q57813676-8ED6D42C-1CAE-47D9-8991-94E1E3DDF32FQ79405688-D5116E88-DEA6-4CDC-96B2-5D4BEDEA0E6CQ79662372-4EF4441C-B534-418F-BBB3-3276506675C8Q80387444-4699C85C-5FDC-44D4-AEF6-B961E42FE78CQ82269841-BAC8C6CF-98FE-457C-8606-83AF9A2FFCB7Q82513093-CD192A0B-C178-4303-A820-9C4F0845BBBCQ83390393-8D66F3F6-4FBE-4DCA-A97A-36634DBB8C35Q83561259-C38D189C-924F-448C-9F6B-93B5DCFFC2E4Q84588656-DFF68835-275E-46BA-B0DB-E5B230E85760Q84868119-F50167E5-890E-4D2D-B77B-34562294141BQ85899207-75972203-C685-4B69-BCE9-1251F010FB10Q92138979-EBCEA518-E62D-46DA-9BB1-ECD27A78D3ADQ92501444-53FF8BDD-E9ED-452A-A861-4A7D2F7FFA18Q92917088-63893EC1-A587-43C0-9AC7-5023A7F4F6B8Q96429630-E9ED7577-67DC-46D5-BAB5-B95DBC91D6A3
P50
description
onderzoeker
@nl
researcher, ORCID id # 0000-0002-9979-305X
@en
name
Jungkweon Choi
@ast
Jungkweon Choi
@en
Jungkweon Choi
@es
Jungkweon Choi
@nl
type
label
Jungkweon Choi
@ast
Jungkweon Choi
@en
Jungkweon Choi
@es
Jungkweon Choi
@nl
prefLabel
Jungkweon Choi
@ast
Jungkweon Choi
@en
Jungkweon Choi
@es
Jungkweon Choi
@nl
P106
P31
P496
0000-0002-9979-305X