Tryptophan phosphorescence studies of the D-galactose/ D-glucose-binding protein from Escherichia coli provide a molecular portrait with structural and dynamics features of the protein
Tryptophan phosphorescence studies of the D-galactose/ D-glucose-binding protein from Escherichia coli provide a molecular portrait with structural and dynamics features of the protein(589 views) D'Auria S, Varriale A, Gonnelli M, Saviano M, Staiano M, Rossi M, Strambini GB
J Proteome Res (ISSN: 1535-3893), 2007; 6(4): 1306-1312.
Keywords: D-Galactose D-Glucose-Binding Protein, Phosphorescence, Protein Conformation, Protein Dynamics, Tryptophan, Arginine, Asparagine, Galaptin, Article, Controlled Study, Escherichia Coli, Molecular Biology, Nonhuman, Priority Journal, Protein Analysis, Protein Structure, Calcium, Crystallography, X-Ray, Escherichia Coli Proteins, Luminescent Measurements, Monosaccharide Transport Proteins, Spectrometry, Fluorescence,
Affiliations: *** IBB - CNR ***
Istituto di Biochimica Delle Proteine, CNR, Via Pietro Castellino, 111, 80131 Naples, Italy
Istituto di Biofisica, CNR, Via Moruzzi 1, 56124 Pisa, Italy
Istituto di Biostruttura e Bioimmagini, CNR, Napoli, Italy
Institute of Protein Biochemistry, Italian National Research Council, Via Pietro Castellino, 111, 80131 Naples, Italy
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Tryptophan phosphorescence studies of the D-galactose/ D-glucose-binding protein from Escherichia coli provide a molecular portrait with structural and dynamics features of the protein
Tryptophan phosphorescence studies of the D-galactose/ D-glucose-binding protein from Escherichia coli provide a molecular portrait with structural and dynamics features of the protein
No results.
Tryptophan phosphorescence studies of the D-galactose/ D-glucose-binding protein from Escherichia coli provide a molecular portrait with structural and dynamics features of the protein