Ultrafast and low barrier motions in the photoreactions of the green fluorescent protein.

doi:10.1074/jbc.M505473200

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Article

Ultrafast and low barrier motions in the photoreactions of the green fluorescent protein.

The Journal of biological chemistry - 30 Sept 2005

van Thor Jasper J, Georgiev Georgi Y, Towrie Michael, Sage J Timothy

Abstract excerpt

Green fluorescent protein (GFP) fluoresces efficiently under blue excitation despite major electrostatic rearrangements resulting from photoionization of the chromophore and neutralization of Glu-222. A competing phototransformation process, which ionizes the chromophore and decarboxylates Glu-222, mimics the electrostatic and structural changes in the fluorescence photocycle. Structural and spectroscopic...

Topics

Bacterial Proteins
Cold Temperature
Crystallography, X-Ray
Decarboxylation
Fluorescence
Glutamine
Green Fluorescent Proteins
Hydrogen Bonding
Light
Luminescent Proteins
Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Structure

Motion

Mutation

Oxygen

Protein Conformation

Spectrophotometry, Infrared

Static Electricity

Source

Open in PubMed

Identifiers

PMID: 16033764
DOI: 10.1074/jbc.M505473200

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