title: Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD.
abstract: 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).
authors: Department of Chemistry & Chemical Biology, Northeastern University, Boston, USA.
authors: Jaylene N
authors: JN
authors: Ollivierre
authors: David E
authors: DE
authors: Budil
authors: Penny J
authors: PJ
authors: Beuning
mesh_terms: D004259:DNA-Directed DNA Polymerase / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013014:SOS Response, Genetics; D013816:Thermodynamics
chemical_list: D029968:Escherichia coli Proteins; D004259:DNA-Directed DNA Polymerase; C055218:UmuD protein, E coli