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A simple method for the determination of deuterium incorporation into nonexchangeable (C-bonded) positions of RNA and protein components of the Escherichia coli ribosome at biosynthetic deuteration has been proposed using small-angle neutron scattering. The theory of the method is based on the joint use of two measurements: one of them is the dependence of neutron scattering intensity at zero angle on the contrast; the second is the dependence of the radius of gyration on the contrast. The main advantage of the method over the standard procedure is that it requires neither separation of the ribosome into RNA and protein components nor a subsequent time-consuming analysis of the hydrolysis products by nuclear magnetic resonance or mass spectrometry.