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Der Zusammenhang fundamentaler Symmetriestrukturen mit dem Zugang moderner Naturwissenschaften zur abstrakten Beschreibung komplexer Systeme wird dargestellt. Beginnend mit der geometrischen Symmetrie der Schneeflocke und dem symmetrietheoretischen Ansatz in Platons Timaios wird der symmetrietheoretische Ansatz moderner Naturwissenschaften exemplifiziert und analysiert. Die mathematische Abstraktion wird als reduktionistische Methode verstanden.
Am 27. und 28. September 2005 tagten Historiker und Philosophen der Mathematik und Naturwissenschaften in Frankfurt a.M. im Gebäude des Physikalischen Vereins. Eine Besonderheit des Internationalen Symposiums war der Dialog mit Vertretern der aktuellen Grundlagendebatte der Basiswissenschaft Physik. In zwölf Vorträgen wurden an zwei Tagen Raum- und Zeitkonzeptionen bedeutender Naturphilosophen der letzten 400 Jahre vorgestellt. Naturwissenschaftshistoriker rekonstruierten die Entwürfe von Giordano Bruno, Marin Mersenne, René Descartes, Otto von Guericke, Baruch Spinoza, Gottfried Wilhelm Leibniz, Isaac Newton und Leonhard Euler, während Grundlagentheoretiker der Physik einen Überblick über eigene Konzeptionen mit einem systematischen Anschluss an die Denktraditionen vorführten. Die Tagung wurde von der Fritz Thyssen Stiftung gefördert sowie vom Förderverein des Frankfurter Institutes für Geschichte der Naturwissenschaften "Arbor Scientiarum" und dem Physikalischen Verein finanziell unterstützt. ...
The paper will focus on the early texts of Galileo Galilei (1613~1623) and Daniel Bernoulli (1738) as examples of pure combinatorical analysis and perspectively considerations within the mathematical discipline of probability theory. It is argued that Bernoulli's approach needed to be developed further in order to achieve a successful and satisfactory theory of risk. In modern economy the need for a proper definition of a notion of risk is seen and currently discussed within the frame of ISO standards. But as already mentioned this interest is mainly owed to the governmental demands of the Basel II and Solvency standards and therefore an external demand. On the other hand an intrinsic understanding of the meaning of risk, as could be provided by a conclusive theory, could lead to a better success in modelling various risks and help to achieve better prognosis.
Symmetrie
(1997)
The highly infectious disease COVID-19 caused by the Betacoronavirus SARS-CoV-2 poses a severe threat to humanity and demands the redirection of scientific efforts and criteria to organized research projects. The international COVID19-NMR consortium seeks to provide such new approaches by gathering scientific expertise worldwide. In particular, making available viral proteins and RNAs will pave the way to understanding the SARS-CoV-2 molecular components in detail. The research in COVID19-NMR and the resources provided through the consortium are fully disclosed to accelerate access and exploitation. NMR investigations of the viral molecular components are designated to provide the essential basis for further work, including macromolecular interaction studies and high-throughput drug screening. Here, we present the extensive catalog of a holistic SARS-CoV-2 protein preparation approach based on the consortium’s collective efforts. We provide protocols for the large-scale production of more than 80% of all SARS-CoV-2 proteins or essential parts of them. Several of the proteins were produced in more than one laboratory, demonstrating the high interoperability between NMR groups worldwide. For the majority of proteins, we can produce isotope-labeled samples of HSQC-grade. Together with several NMR chemical shift assignments made publicly available on covid19-nmr.com, we here provide highly valuable resources for the production of SARS-CoV-2 proteins in isotope-labeled form.
The SARS-CoV-2 genome encodes for approximately 30 proteins. Within the international project COVID19-NMR, we distribute the spectroscopic analysis of the viral proteins and RNA. Here, we report NMR chemical shift assignments for the protein Nsp3b, a domain of Nsp3. The 217-kDa large Nsp3 protein contains multiple structurally independent, yet functionally related domains including the viral papain-like protease and Nsp3b, a macrodomain (MD). In general, the MDs of SARS-CoV and MERS-CoV were suggested to play a key role in viral replication by modulating the immune response of the host. The MDs are structurally conserved. They most likely remove ADP-ribose, a common posttranslational modification, from protein side chains. This de-ADP ribosylating function has potentially evolved to protect the virus from the anti-viral ADP-ribosylation catalyzed by poly-ADP-ribose polymerases (PARPs), which in turn are triggered by pathogen-associated sensing of the host immune system. This renders the SARS-CoV-2 Nsp3b a highly relevant drug target in the viral replication process. We here report the near-complete NMR backbone resonance assignment (1H, 13C, 15N) of the putative Nsp3b MD in its apo form and in complex with ADP-ribose. Furthermore, we derive the secondary structure of Nsp3b in solution. In addition, 15N-relaxation data suggest an ordered, rigid core of the MD structure. These data will provide a basis for NMR investigations targeted at obtaining small-molecule inhibitors interfering with the catalytic activity of Nsp3b.
