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Shortcut to protein portraits

Media Releases Research with light Biology

All living organisms, from bacteria to humans, rely on proteins to perform their vital functions. How these proteins accomplish their tasks depends on their structure. Researchers from the Paul Scherrer Institute have now devised a novel method to determine the crystal structure of proteins using X-ray light, which could also hasten the development of new drugs in future. The study will be published in the journal Nature Methods on 15 December.

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How the body distinguishes between self and non-self – important structures explained

Media Releases Biology Research with light

Like a shredder, the immunoproteasome cuts down proteins into peptides that are subsequently presented on the cellular surface. The immune system can distinguish between self and non-self peptides and selectively kills cells that present non-self peptides at their surface. In autoimmune diseases, this mechanism is deregulated. However, inhibition of the immunoproteasome may alleviate disease symptoms and progression. With the help of measurements taken at the Paul Scherer Institute, scientists have now succeeded in determining the first structure of an immunoproteasome.

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Model of the eukaryotic ribosome (taken from Klinge et al.)

New insights into the cell’s protein factory

Eukaryotic ribosomes are among the most complex cellular machineries of the cell. These large macromolecular assemblies are responsible for the production of all proteins and are thus of pivotal importance to all forms of life. Two independent research groups at the ETH Zürich and the Institute of Genetics and Molecular and Cellular Biology in Strasbourg have obtained new insights into the atomic structure of the eukaryotic ribosome. The results have been published in the journal Science.

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Dem Rätsel der Centriolen-Bildung auf der Spur

Media Releases Health Innovation Biology Research with light

In menschlichen Zellen finden sich stammesgeschichtlich sehr alte Funktionseinheiten, die als Centriolen bezeichnet werden. Ein Forscherteam vom PSI und der ETH Lausanne hat nun erstmals ein Modell für die Bildung der Centriolen vorgestellt. Das erstaunende Ergebnis ist, dass die Neuner-Symmetrie des Centriols durch die Fähigkeit eines einzelnen Proteins sich selbst zu organisieren zustande kommt.This news release is only available in French and German.

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This is a text from the PSI media archive. The contents may be out-of-date.