Papers by Mauro Rinaldelli
Development of software tools for protein structural and dynamic characterization
NMR crystallography on paramagnetic systems: solved and open issues
CrystEngComm, 2013
Teoria Computazionale dei Nodi
cs.unicam.it
... Riccardo Piergallini per la disponibilità e l'aiuto che mi ha dato. Desidero inoltre... more ... Riccardo Piergallini per la disponibilità e l'aiuto che mi ha dato. Desidero inoltre ringraziare enormemente i miei due fratelli Bruno e Giam-paolo, i miei genitori e zia Claudia per il loro altrettanto grande supporto, sia morale che pratico, sotto forma di preziosi consigli, paziente ...
FANTEN: a new web-based interface for the analysis of magnetic anisotropy-induced NMR data
Journal of biomolecular NMR, 2015
Pseudocontact shifts (PCSs) and residual dipolar couplings (RDCs) arising from the presence of pa... more Pseudocontact shifts (PCSs) and residual dipolar couplings (RDCs) arising from the presence of paramagnetic metal ions in proteins as well as RDCs due to partial orientation induced by external orienting media are nowadays routinely measured as a part of the NMR characterization of biologically relevant systems. PCSs and RDCs are becoming more and more popular as restraints (1) to determine and/or refine protein structures in solution, (2) to monitor the extent of conformational heterogeneity in systems composed of rigid domains which can reorient with respect to one another, and (3) to obtain structural information in protein-protein complexes. The use of both PCSs and RDCs proceeds through the determination of the anisotropy tensors which are at the origin of these NMR observables. A new user-friendly web tool, called FANTEN (Finding ANisotropy TENsors), has been developed for the determination of the anisotropy tensors related to PCSs and RDCs and has been made freely available t...
Journal of the American Chemical Society, 2012
Pseudocontact shifts (PCSs) measured by solid-state NMR spectroscopy (SS-NMR) on microcrystalline... more Pseudocontact shifts (PCSs) measured by solid-state NMR spectroscopy (SS-NMR) on microcrystalline powders of a paramagnetic metalloprotein permit NMR crystallography. Along with other restraints for SS-NMR experiments, the protein molecular structure as well as the correct crystal packing are obtained.
Classical and Quantum Gravity, 2009
By definition a spacetime is stably causal if it is possible to widen the light cones all over th... more By definition a spacetime is stably causal if it is possible to widen the light cones all over the spacetime without spoiling causality. We prove that if the spacetime is at least non-total imprisoning then it is stably causal provided the light cones can be widened outside any arbitrarily large compact set, i.e. in a neighborhood of infinity, without spoiling causality. Furthermore, we prove that the new causality level 'compact stable causality' can be obtained as the antisymmetry condition of a new causal relation which we identify, but it cannot be obtained as a causal stability condition with respect to a topology on metrics. The difference between stable causality and compact stable causality is shown to follow from the fact that Geroch's interval topology on the space of conformal metrics of M is not Fréchet-Urysohn (in fact it is not even T -sequential). In particular we prove that (compact) stably causal metrics are those in the (sequential) interior of the set of chronological metrics. Finally, contrary to previous claims it is shown that stable causality with respect to the C 0 fine topology on metrics leads to the usual notion of stable causality.
Acta Crystallographica Section D Biological Crystallography, 2014
The program REFMAC5 from CCP4 was modified to allow the simultaneous use of X-ray crystallographi... more The program REFMAC5 from CCP4 was modified to allow the simultaneous use of X-ray crystallographic data and paramagnetic NMR data (pseudocontact shifts and selforientation residual dipolar couplings) and/or diamagnetic residual dipolar couplings. Incorporation of these long-range NMR restraints in REFMAC5 can reveal differences between solid-state and solution conformations of molecules or, in their absence, can be used together with X-ray crystallographic data for structural refinement. Since NMR and X-ray data are complementary, when a single structure is consistent with both sets of data and still maintains reasonably 'ideal' geometries, the reliability of the derived atomic model is expected to increase. The program was tested on five different proteins: the catalytic domain of matrix metalloproteinase 1, GB3, ubiquitin, free calmodulin and calmodulin complexed with a peptide. In some cases the joint refinement produced a single model consistent with both sets of observations, while in other cases it indicated, outside the experimental uncertainty, the presence of different protein conformations in solution and in the solid state.
ChemInform Abstract: NMR Crystallography on Paramagnetic Systems. Solved and Open Issues
ChemInform, 2014
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Papers by Mauro Rinaldelli