Time-resolved fluorescence study of azurin variants: conformational heterogeneity and tryptophan mobility.

doi:10.1016/S0006-3495(98)77688-X

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Article

Time-resolved fluorescence study of azurin variants: conformational heterogeneity and tryptophan mobility.

Biophysical journal - 1 Nov 1998

Kroes S J, Canters G W, Gilardi G, van Hoek A, Visser A J

Abstract excerpt

Time-resolved fluorescence and time resolved fluorescence anisotropy studies have been performed on wild-type azurin from Pseudomonas aeruginosa and two variants to study the mobility of Trp48. The two azurin variants in which the microenvironment of Trp48 was changed comprised the single mutatio...

Topics

Azurin
Bacterial Proteins
Fluorescence Polarization
Hydrogen-Ion Concentration
Kinetics
Metalloproteins
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Protein Conformation
Pseudomonas aeruginosa
Tryptophan

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