Issue 12, 2011
From the journal:

Molecular BioSystems

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

Jaylene N. Ollivierre,a   David E. Budila  and  Penny J. Beuning*ab  

* Corresponding authors

a Department of Chemistry & Chemical Biology, Northeastern University, Boston, USA
E-mail: beuning@neu.edu
Fax: +1-617-373-8795
Tel: +1-617-373-2865

b Center for Interdisciplinary Research on Complex Systems, Northeastern University, Boston, USA

Abstract

Electron paramagnetic resonance (EPR) spectroscopy was used to probe the conformational dynamics of the N-terminal arms of the umuDgene products. We determined that the arms of UmuD2 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.

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

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Article information

DOI
https://doi.org/10.1039/C1MB05334E
Article type
Communication
Submitted
12 Aug 2011
Accepted
12 Sep 2011
First published
05 Oct 2011

Mol. BioSyst., 2011,7, 3183-3186

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

J. N. Ollivierre, D. E. Budil and P. J. Beuning, Mol. BioSyst., 2011, 7, 3183 DOI: 10.1039/C1MB05334E

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