Mechanismusabhängige Regulation der ultraschnellen Dynamik von Wasser an Grenzflächen in Komplexen mit intrinsisch ungeordneten Proteinen

Chowdhury, Aritra; Kovalenko, Sergey A.; Aramburu, Iker Valle; Tan, Piau Siong; Érnsting, N. P.; Lemke, Edward A.

doi:10.1002/ange.201813354

Angewandte Chemie

2019

DOI: 10.1002/ange.201813354

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Mechanismusabhängige Regulation der ultraschnellen Dynamik von Wasser an Grenzflächen in Komplexen mit intrinsisch ungeordneten Proteinen

Aritra Chowdhury

Sergey A. Kovalenko

Iker Valle Aramburu

et al.

Abstract: In diesem Beitrag wird das

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Cited by 2 publications

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Hydrogen‐Bond Free Energy of Local Biological Water

Park

Lee

et al. 2020

Angewandte Chemie

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Here,w ep ropose an experimental methodology based on femtosecond-resolved fluorescence spectroscopyt o measure the hydrogen (H)-bond free energy of water at protein surfaces under isothermal conditions.Ademonstration was conducted by installing anon-canonical isostere of tryptophan (7-azatryptophan) at the surface of ac oiled-coil protein to exploit the photoinduced proton transfer of its chromophoric moiety,7-azaindole.The H-bond free energy of this biological water was evaluated by comparing the rates of proton transfer, sensitive to the hydration environment, at the protein surface and in bulk water,a nd it was found to be higher than that of bulk water by 0.4 kcal mol À1 .T he free-energy difference is dominated by the entropic cost in the H-bond network among water molecules at the hydrophilic and charged protein surface. Our study opens ad oor to accessing the energetics and dynamics of local biological water to give insight into its roles in protein structure and function.

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Hydrogen‐Bond Free Energy of Local Biological Water

Park

Lee

et al. 2020

Angewandte Chemie

View full text Add to dashboard Cite

show abstract

Hydrogen‐Bond Free Energy of Local Biological Water

Park

Lee

et al. 2020

Angew Chem Int Ed

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Here, we propose an experimental methodology based on femtosecond‐resolved fluorescence spectroscopy to measure the hydrogen (H)‐bond free energy of water at protein surfaces under isothermal conditions. A demonstration was conducted by installing a non‐canonical isostere of tryptophan (7‐azatryptophan) at the surface of a coiled‐coil protein to exploit the photoinduced proton transfer of its chromophoric moiety, 7‐azaindole. The H‐bond free energy of this biological water was evaluated by comparing the rates of proton transfer, sensitive to the hydration environment, at the protein surface and in bulk water, and it was found to be higher than that of bulk water by 0.4 kcal mol−1. The free‐energy difference is dominated by the entropic cost in the H‐bond network among water molecules at the hydrophilic and charged protein surface. Our study opens a door to accessing the energetics and dynamics of local biological water to give insight into its roles in protein structure and function.

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Mechanismusabhängige Regulation der ultraschnellen Dynamik von Wasser an Grenzflächen in Komplexen mit intrinsisch ungeordneten Proteinen

Abstract: In diesem Beitrag wird das

Cited by 2 publications

References 30 publications

Hydrogen‐Bond Free Energy of Local Biological Water

Hydrogen‐Bond Free Energy of Local Biological Water

Hydrogen‐Bond Free Energy of Local Biological Water

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