Ligand-induced changes in the conformational dynamics of a bacterial cytotoxic endonuclease.

Journal article

Knowledge about the conformational dynamics of a protein is key to understanding its biochemical and biophysical properties. In the present work we investigated the dynamic properties of the enzymatic domain of DNase colicins via time-resolved fluorescence and anisotropy decay analysis in combination with steady-state acrylamide quenching experiments. The dynamic properties of the apoenzyme were compared to those of the E9 DNase ligated to the transition metal ion Zn(2+) and the natural inhib...

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Authors: van den Bremer, E; Keeble, A; Visser, A; van Hoek, A; Kleanthous, K

• Journal: Biochemistry
• Volume: 43
• Issue: 14
• Pages: 4347-4355
• Publication date: 2004-04-01
• DOI: 10.1021/bi049929c
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Protein Structure, Tertiary; Thermodynamics; Binding Sites; Mutagenesis, Site-Directed; Spectrometry, Fluorescence; Ligands; Colicins; Fluorescence Polarization; Zinc; Deoxyribonucleases; Phenylalanine; Tryptophan; Bacterial Proteins; Protein Conformation; Bacterial Toxins; Solvents