Background: Centralized collection and processing of healthcare data across national borders pose significant challenges, including privacy concerns, data heterogeneity and legal barriers. To address some of these challenges, we formed an interdisciplinary consortium to develop a feder-ated health data network, comprised of six institutions across five countries, to facilitate Nordic-Baltic cooperation on secondary use of health data. The objective of this report is to offer early insights into our experiences developing this network. Methods: We used a mixed-method ap-proach, combining both experimental design and implementation science to evaluate the factors affecting the implementation of our network. Results: Technically, our experiments indicate that the network functions without significant performance degradation compared to centralized simu-lation. Conclusion: While use of interdisciplinary approaches holds a potential to solve challeng-es associated with establishing such collaborative networks, our findings turn the spotlight on the uncertain regulatory landscape playing catch up and the significant operational costs.

We apply HMMs to the problem of modeling exons, intronsand detecting splice sites in the human genome. Our most interesting result so far is the detection of particular oscillatory patterns,with a minimal period ofroughly 10 nucleotides, that seem to be characteristic of exon regions and may have significant biological implications.

Human genes are not continuous but rather consist of short coding regions (exons) interspersed with highly variable non-coding regions (introns). We apply HMMs to the problem of modeling exons, introns and detecting splice sites in the human genome. Our most interesting result so far is the detection of particular oscillatory patterns, with a minimal period ofroughly 10 nucleotides, that seem to be characteristic of exon regions and may have significant biological implications.

One current aim of molecular biology is determination of the (3D) tertiary structures ofproteins in their folded native state from their sequences of amino acid 523 524 Fredholm, Bohr, Bohr, Brunak, Cotterill, Lautrup, and Thtersen residues. Since Kendrew & Perutz solved the first protein structures, myoglobin and hemoglobin, and explained from the discovered structures how these proteins perform their function, it has been widely recognized that protein function is intimately linkedwith protein structure[l]. Within the last two decades X-ray crystallographers have solved the 3-dimensional (3D) structures of a steadily increasing number of proteins in the crystalline state, and recently 2D-NMR spectroscopy has emerged as an alternative method for small proteins in solution. Today approximately three hundred 3D structures have been solved by these methods, although only about half of them can be considered as truly different, and only around a hundred of them are solved at high resolution (that is, less than 2A). The number of protein sequences known today is well over 20,000, and this number seems to be growing at least one order of magnitude faster than the number of known 3D protein structures. Obviously, it is of great importance to develop tools that can predict structural aspects of proteins on the basis of knowledge acquired from known 3D structures.

Since Kendrew & Perutz solved the first protein structures, myoglobin and hemoglobin, and explained from the discovered structures how these proteins perform their function, it has been widely recognized that protein function is intimately linked with protein structure[l]. Within the last two decades X-ray crystallographers have solved the 3-dimensional (3D) structures of a steadily increasing number of proteins in the crystalline state, and recently 2D-NMR spectroscopy has emerged as an alternative method for small proteins in solution. Today approximately three hundred 3D structures have been solved by these methods, although only about half of them can be considered as truly different, and only around a hundred of them are solved at high resolution (that is, less than 2A). The number of protein sequences known today is well over 20,000, and this number seems to be growing at least one order of magnitude faster than the number of known 3D protein structures. Obviously, it is of great importance to develop tools that can predict structural aspects of proteins on the basis of knowledge acquired from known 3D structures.