In an article in the latest issue of “Kemisk Tidskrift” Jonas Baranduns “tiny” ribosome structure is shown together with an update on ISB in Umeå!!
About Magnus Wolf-Watz
This author has yet to write their bio.Meanwhile lets just say that we are proud Magnus Wolf-Watz contributed a whooping 8 entries.
Entries by Magnus Wolf-Watz
In a computational study by ISB member Kwangho Nam (Umeå and UT Arlington) and Martin Karplus (Harvard University) a detailed model has been developed for the coupling between rotary motion and ATP hydrolysis in F1-ATPase. The model predicts that F1-ATPase functions at near its maximum possible efficiency. The finding is published in PNAS. https://www.pnas.org/content/116/32/15924.long
In an ISB effort the research groups lead by Anna Linusson, Elisabeth Sauer-Eriksson and Magnus Wolf-Watz has discovered a key event in activation of the essential enzyme adenylate kinase. It was discovered that the large-scale and activating conformational change triggered by ATP binding is nucleated by a strong cation-PI interaction formed between the cationic sidechain […]
We are happy to announce that the Kempe foundation is funding an ISB postdoc program with two fellowships 2019 and three fellowships 2020. Running costs are included for the positions. The program will fund new constellations that tackle interdisciplinary structural biology projects. For more information please go to the page ISB Postdoctoral program.
Professor Erik Johansson has published an article in Nature Communications named “Structural consequence of the most frequently recurring cancer-associated substitution in DNA polymerase epsilon“. The study was a collaboration with Uppsala University and University of Nebraska Medical Center. The article can be found at: “www.nature.com/articles/s41467-018-08114-9”
Magnus Wolf-Watz was named professor in biophysical chemistry on May 1:st 2018.
This paper from the Wolf-Watz lab describes the discovery of a fundamentally new mechanism underlying protein-protein interactions. The chaperone-binding domain of the Yersinia effector protein YopH was found to lose its globular structure upon formation of a wrap-around architecture with its chaperone SycH. The mechanism is best described as a coupled binding and disordering event. […]
We have an opening for a postdoc in enzyme dynamics. The salary is provided as a fellowship.