Computational aspects of NMR in structural biology

The efficient integration of many different physical techniques is required in order to maximize the reliability of structural biology studies. The combination of the data provided from these heterogeneous techniques is not as straightforward as it sometimes appears and the quality of the scientific results is often limited by the level of expertise of the scientist dealing with them. Hence, it is on the large research infrastructures to encode their specific high-level know-how into user-friendly computational tools for the combination of different informative sources that need to be made available to the wider scientific community. As members of the NMR community, we focused on giving our contribution to extend the applicability of paramagnetic-assisted solution NMR in the context of structural biology, exploring all the possibilities that all these data offer. During the last decades, pseudo-contact shifts (PCSs) and residual dipolar couplings (RDCs) arising from the paramagnetic centers present in proteins gained a relevant role in the characterization of biological systems and, nowadays, they are routinely measured in several laboratories. The increasing popularity of these restraints mostly resides on their wide applicability such as determination, refinement and validation of protein structures in solution. Besides this, PCSs and RDCs stand out among NMR-based restrains, for their intrinsic property of giving long-range structural information, which results of particular interest in the study of multi-domain proteins and protein-protein complexes, detecting the relative arrangement and/or the mobility effects between the different structural units.