Infrared investigation of poly-L-histidine structure dependent on protonation

7Li-NMR and FTIR studies of lithium, potassium, rubidium, and cesium complexes with ionophore lasalocid in solution.

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Proton relay system in the active site of maltodextrinphosphorylase via hydrogen bonds with large proton polarizability: an FT-IR difference spectroscopy study.

European biophysics journal : EBJ·1999

Fourier transform infrared spectroscopic studies of proton transfer processes and the dissociation of Zn2+-bound water in alcohol dehydrogenases.

European journal of biochemistry·1997

Model molecules for the active centre of alcoholdehydrogenases--an FT-IR study.

Biochemical and biophysical research communications·1997

Aspartic proteinases: Fourier transform infrared spectroscopic studies of a model of the active side.

Biophysical journal·1996

A model molecule of the hydrogen-bonded chain in the active site of bacteriorhodopsin.

Biochemical and biophysical research communications·1996

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Inorganic chemistry·2026

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Angewandte Chemie (International ed. in English)·2026

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Frontiers in neuroscience·2026

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Related Experiment Videos

Infrared investigation of poly-L-histidine structure dependent on protonation

Related Concept Videos

7Li-NMR and FTIR studies of lithium, potassium, rubidium, and cesium complexes with ionophore lasalocid in solution.

Proton relay system in the active site of maltodextrinphosphorylase via hydrogen bonds with large proton polarizability: an FT-IR difference spectroscopy study.

Fourier transform infrared spectroscopic studies of proton transfer processes and the dissociation of Zn2+-bound water in alcohol dehydrogenases.

Model molecules for the active centre of alcoholdehydrogenases--an FT-IR study.

Aspartic proteinases: Fourier transform infrared spectroscopic studies of a model of the active side.

A model molecule of the hydrogen-bonded chain in the active site of bacteriorhodopsin.

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Infrared investigation of poly-L-histidine structure dependent on protonation

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