Spin-echo verification of the molecular dynamics simulations of RecA protein from D.radiodurans
Homologous recombination protein RecA is the key DNA repair enzyme in bacteria. Although the structure and function of a RecA and its analogues (such as RadA in archae and Rad51 in higher eucariotes) are very well studied, the detailed molecular mechanisms for the enzymatic activity of this family of proteins is still uncertain. As this enzyme works in the polymerized form bound to a relatively long stretch of DNA, large-scale conformational flexibility plays an important role in its function. Functional subdomain motion in RecA protein and its inference on the protein filament flexibility on the larger scale have been identifyed by computer simulation of molecular dynamics. We propose to obtain an experimental verification for the molecular dynamics model by neutron spin-echo.
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LEBEDEV Dmitry; FALUS Peter; GORKOV Dmytro; SHVETSOV Alexey and VOROBIEV Alexei. (2013). Spin-echo verification of the molecular dynamics simulations of RecA protein from D.radiodurans. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-698
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