EXO 0748-676 Rules out Soft Equations of State for Neutron Star Matter

The interiors of neutron stars contain matter at very high densities, in a state that differs greatly from those found in the early universe or achieved at terrestrial experiments. Matter in these conditions can only be probed through astrophysical observations that measure the mass and radius of neutron stars with sufficient precision. Here I report for the first time a unique determination of the mass and radius of the neutron star EXO 0748-676, which appears to rule out all the soft equations of state of neutron star matter. If this object is typical, then condensates and unconfined quarks do not exist in the centers of neutron stars.Comment: To appear in Nature, press embargo until publicatio

Homology Inference of Protein-Protein Interactions via Conserved Binding Sites

The coverage and reliability of protein-protein interactions determined by high-throughput experiments still needs to be improved, especially for higher organisms, therefore the question persists, how interactions can be verified and predicted by computational approaches using available data on protein structural complexes. Recently we developed an approach called IBIS (Inferred Biomolecular Interaction Server) to predict and annotate protein-protein binding sites and interaction partners, which is based on the assumption that the structural location and sequence patterns of protein-protein binding sites are conserved between close homologs. In this study first we confirmed high accuracy of our method and found that its accuracy depends critically on the usage of all available data on structures of homologous complexes, compared to the approaches where only a non-redundant set of complexes is employed. Second we showed that there exists a trade-off between specificity and sensitivity if we employ in the prediction only evolutionarily conserved binding site clusters or clusters supported by only one observation (singletons). Finally we addressed the question of identifying the biologically relevant interactions using the homology inference approach and demonstrated that a large majority of crystal packing interactions can be correctly identified and filtered by our algorithm. At the same time, about half of biological interfaces that are not present in the protein crystallographic asymmetric unit can be reconstructed by IBIS from homologous complexes without the prior knowledge of crystal parameters of the query protein