We propose a novel approach to detect the binding between proteins making use
of the anomalous diffraction of natively present heavy elements inside the
molecule 3D structure. In particular, we suggest considering sulfur atoms
contained in protein structures at lower percentages than the other atomic
species. Here, we run an extensive preliminary investigation to probe both the
feasibility and the range of usage of the proposed protocol. In particular, we
(i) analytically and numerically show that the diffraction patterns produced by
the anomalous scattering of the sulfur atoms in a given direction depend
additively on the relative distances between all couples of sulfur atoms. Thus
the differences in the patterns produced by bound proteins with respect to
their non-bonded states can be exploited to rapidly assess protein complex
formation. Next, we (ii) carried out analyses on the abundances of sulfurs in
the different proteomes and molecular dynamics simulations on a representative
set of protein structures to probe the typical motion of sulfur atoms. Finally,
we (iii) suggest a possible experimental procedure to detect protein-protein
binding. Overall, the completely label-free and rapid method we propose may be
readily extended to probe interactions on a large scale even between other
biological molecules, thus paving the way to the development of a novel field
of research based on a synchrotron light source.Comment: 9 pages, 4 figure