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

Mol Biosyst. 2011 Dec;7(12):3183-6. doi:10.1039/c1mb05334e. Epub 2011 Oct 05

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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).

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

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