Enzyme activity and structural features of three single-domain phloem cyclophilins from Brassica napus

Cyclophilins (CYPs) are a group of ubiquitous prolyl cis/trans isomerases (PPIases). It was shown that plants possess the most diverse CYP families and that these are abundant in the phloem long-distance translocation stream. Since phloem exudate showed PPIase activity, three single-domain CYPs that occur in phloem samples from Brassica napus were characterised on functional and structural levels. It could be shown that they exhibit isomerase activity and that this activity is controlled by a redox regulation mechanism, which has been postulated for divergent CYPs. The structure determination by small-angle X-ray scattering experiments revealed a conserved globular shape. In addition, the high-resolution crystal structure of BnCYP19-1 was resolved and refined to 2.0 Å resolution, and the active sites of related CYPs as well as substrate binding were modelled. The obtained data and results support the hypothesis that single domain phloem CYPs are active phloem PPIases that may function as chaperones

b and c spectroscopy at LHCb

The LHCb experiment is designed to study the decays and properties of heavy flavoured hadrons produced in the forward region from pp collisions at the CERN Large Hadron Collider. It has recorded the world's largest data sample of beauty and charm hadrons, enabling precise studies into the spectroscopy of such particles, including discoveries of new states and measurements of their properties such as masses, width and quantum numbers. The latest results in this area are reviewed

Receptor dimerization dynamics as a regulatory valve for plasticity of type I interferon signaling.

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