Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD

Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD

Electron paramagnetic resonance (EPR) spectroscopy was used to probe the conformational dynamics of the N-terminal arms of the umuD gene products. We determined that the arms of UmuD(2) display a large degree of motion, are largely unbound from the globular C-terminal domain, and that the free energ...

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Veröffentlicht in:Molecular bioSystems 2011-12, Vol.7 (12), p.3183
Hauptverfasser: Ollivierre, Jaylene N, Budil, David E, Beuning, Penny J
Format: Artikel
Sprache:eng
Schlagworte:
DNA-Directed DNA Polymerase - chemistry
Electron Spin Resonance Spectroscopy
Escherichia coli
Escherichia coli Proteins - chemistry
Models, Molecular
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
SOS Response (Genetics)
Thermodynamics
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Zusammenfassung:Electron paramagnetic resonance (EPR) spectroscopy was used to probe the conformational dynamics of the N-terminal arms of the umuD gene products. We determined that the arms of UmuD(2) display a large degree of motion, are largely unbound from the globular C-terminal domain, and that the free energy of dissociation is +2.1 kJ mol(-1).
ISSN:1742-206X
1742-2051
DOI:10.1039/c1mb05334e