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Veröffentlich: 13. Januar 2023 (vor 2 Monaten )

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Artcut 2009 Cd2

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Does anyone use Oracle (or another DBMS) for ASP.NET development?

Does anyone develop ASP.NET applications with Oracle (or a compatible DBMS) databases for the web? It’s not necessarily a question of ORM, but are there any downsides to using Oracle in a.NET development scenario? Specifically, what additional libraries might need to be set up?

Yes, we do, but we use Oracle and SQLServer instead of oracle and sqlserver. We use the free version of ADO.NET Data Services to read our oracle database.
Additionally, there is a swedish team that develops a open source library and database model for ASP.NET that can be used for this purpose. You can look at the code and database model at

Project Summary If we can determine how proteins can switch between order and disorder states on specific timescales, this may have significant implications in the fields of biophysics, biology, and medicine. To elucidate the conformational states of proteins, the fluctuations of inherent structures are often calculated. However, this simple approach may fail to accurately determine the timescales for the rearrangement of proteins. Here, we propose to systematically examine the timescales and mechanisms of protein rearrangement using a combination of time-resolved all-atom molecular dynamics (MD) simulations and linear response theory (LRT). We aim to determine the free energy differences of protein rearrangement in terms of solvation free energies and conformational fluctuations of the protein and water. We will use the Stokesian dynamics to reduce the effect of the solvent. This is accomplished by calculating the friction matrix, which can be written as the sum of the eigenvalues of the imaginary part of the Green’s function of the protein immersed in the solvent. From these friction terms, we can calculate the relaxation timescales of the protein by using LRT. Then, we will consider the effect of the protein’s temperature on the solvent-mediated relaxation timescales. Finally, we will apply these results to proteins with experimental data to determine their extent of dynamic disorder. This new method

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