The Experts below are selected from a list of 137604 Experts worldwide ranked by ideXlab platform
Tahei Tahara - One of the best experts on this subject based on the ideXlab platform.
-
role of coherent low Frequency Motion in excited state proton transfer of green fluorescent protein studied by time resolved impulsive stimulated raman spectroscopy
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (<300 cm–1) in the excited state of GFP, we examined the excited-state structural evolution and the ESPT dynamics within the dephasing time of the low-Frequency vibration. A clear anharmonic vibrational coupling is found between one high-Frequency mode of the chromophore (phenolic CH bend) and a low-Frequency mode at ∼104 cm–1. However, the data show that this low-Frequency Motion does not substantially affect the ESPT dynamics.
-
Role of Coherent Low-Frequency Motion in Excited-State Proton Transfer of Green Fluorescent Protein Studied by Time-Resolved Impulsive Stimulated Raman Spectroscopy.
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (
Tomotsumi Fujisawa - One of the best experts on this subject based on the ideXlab platform.
-
role of coherent low Frequency Motion in excited state proton transfer of green fluorescent protein studied by time resolved impulsive stimulated raman spectroscopy
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (<300 cm–1) in the excited state of GFP, we examined the excited-state structural evolution and the ESPT dynamics within the dephasing time of the low-Frequency vibration. A clear anharmonic vibrational coupling is found between one high-Frequency mode of the chromophore (phenolic CH bend) and a low-Frequency mode at ∼104 cm–1. However, the data show that this low-Frequency Motion does not substantially affect the ESPT dynamics.
-
Role of Coherent Low-Frequency Motion in Excited-State Proton Transfer of Green Fluorescent Protein Studied by Time-Resolved Impulsive Stimulated Raman Spectroscopy.
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (
Hikaru Kuramochi - One of the best experts on this subject based on the ideXlab platform.
-
role of coherent low Frequency Motion in excited state proton transfer of green fluorescent protein studied by time resolved impulsive stimulated raman spectroscopy
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (<300 cm–1) in the excited state of GFP, we examined the excited-state structural evolution and the ESPT dynamics within the dephasing time of the low-Frequency vibration. A clear anharmonic vibrational coupling is found between one high-Frequency mode of the chromophore (phenolic CH bend) and a low-Frequency mode at ∼104 cm–1. However, the data show that this low-Frequency Motion does not substantially affect the ESPT dynamics.
-
Role of Coherent Low-Frequency Motion in Excited-State Proton Transfer of Green Fluorescent Protein Studied by Time-Resolved Impulsive Stimulated Raman Spectroscopy.
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (
Satoshi Takeuchi - One of the best experts on this subject based on the ideXlab platform.
-
role of coherent low Frequency Motion in excited state proton transfer of green fluorescent protein studied by time resolved impulsive stimulated raman spectroscopy
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (<300 cm–1) in the excited state of GFP, we examined the excited-state structural evolution and the ESPT dynamics within the dephasing time of the low-Frequency vibration. A clear anharmonic vibrational coupling is found between one high-Frequency mode of the chromophore (phenolic CH bend) and a low-Frequency mode at ∼104 cm–1. However, the data show that this low-Frequency Motion does not substantially affect the ESPT dynamics.
-
Role of Coherent Low-Frequency Motion in Excited-State Proton Transfer of Green Fluorescent Protein Studied by Time-Resolved Impulsive Stimulated Raman Spectroscopy.
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (
Haruko Hosoi - One of the best experts on this subject based on the ideXlab platform.
-
role of coherent low Frequency Motion in excited state proton transfer of green fluorescent protein studied by time resolved impulsive stimulated raman spectroscopy
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (<300 cm–1) in the excited state of GFP, we examined the excited-state structural evolution and the ESPT dynamics within the dephasing time of the low-Frequency vibration. A clear anharmonic vibrational coupling is found between one high-Frequency mode of the chromophore (phenolic CH bend) and a low-Frequency mode at ∼104 cm–1. However, the data show that this low-Frequency Motion does not substantially affect the ESPT dynamics.
-
Role of Coherent Low-Frequency Motion in Excited-State Proton Transfer of Green Fluorescent Protein Studied by Time-Resolved Impulsive Stimulated Raman Spectroscopy.
Journal of the American Chemical Society, 2016Co-Authors: Tomotsumi Fujisawa, Hikaru Kuramochi, Haruko Hosoi, Satoshi Takeuchi, Tahei TaharaAbstract:Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to Glu222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-Frequency Motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low-Frequency modes (
