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Titlebook: Computational Life Sciences; First International Michael R. Berthold,Robert C. Glen,Ingrid Fischer Conference proceedings 2005 Springer-Ve

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發(fā)表于 2025-3-23 09:56:22 | 只看該作者
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發(fā)表于 2025-3-23 14:07:50 | 只看該作者
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發(fā)表于 2025-3-23 19:53:20 | 只看該作者
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發(fā)表于 2025-3-23 23:45:50 | 只看該作者
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發(fā)表于 2025-3-24 04:55:33 | 只看該作者
BioRegistry: A Structured Metadata Repository for Bioinformatic Databasesnformation, access/availability, and tracking of the metadata. The BioRegistry model and its relationships with the DCMI (Dublin Core Metadata Initiative) are described. Prototypes with various functionalities to feed, maintain and exploit the repository are presented.
16#
發(fā)表于 2025-3-24 10:19:58 | 只看該作者
Robust Perron Cluster Analysis for Various Applications in Computational Life Scienceng of HIV protease inhibitors corresponding to their activity. In theoretical chemistry, PCCA+ is applied to the analysis of metastable ensembles in monomolecular kinetics, which is a tool for RNA folding [21].
17#
發(fā)表于 2025-3-24 11:09:35 | 只看該作者
18#
發(fā)表于 2025-3-24 14:52:50 | 只看該作者
Die Herkunft des Schemas vom Ursprung,avior on the clones, i.e., gains or losses. Frequent itemsets show promising biological expressiveness, can be computed efficiently, and are very flexible. Their visualization provides the biologist with useful information for the discovery of patterns. Also it turns out that the use of (larger) frequent itemsets tends to filter out noise.
19#
發(fā)表于 2025-3-24 21:14:45 | 只看該作者
Strukturwandel der Verteidigungction strategy is first to select the features with higher sensitivities but meanwhile keep the remaining ones, and then refine the selected subset by tentatively substituting some part with fragments of the previously rejected features. The accuracy of our method is validated experimentally on the benchmark microarray datasets.
20#
發(fā)表于 2025-3-25 00:08:03 | 只看該作者
Strukturwandel der industriellen Beziehungensed for chemical stability and only stable oligomers are left as a potential solution. We also discuss theoretical models for the assessment of protein affinity and entropy loss on complex formation, used in stability analysis.
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