Events & News
09/09/2015 Emotionen und das Meer
Fenster zur Wissenschaft
09/17/2015 CoWell Brown Bag Research Seminar
Promotion of Regional Innovation Systems: The Role of Universities and EU Funding Schemes
09/17/2015 MoLife Research Seminar: Prof. Pavel Jungwirth
Beyond Hofmeister: Interactions Between Ions and Proteins in Water
Recently, mechanisms underlying specific ion effects on protein solubility and stability, as expressed in the Hofmeister series of ions, have been firmly established at the molecular level. Further progress in understanding ion-specific effects in biological systems requires, however, to go beyond the simplifying concept of separate anionic and cationic Hofmeister series. What matters is not only the behaviour of individual ions at the protein surface but, to varying extents, also interactions between the salt ions themselves, both near the protein and in the bulk aqueous solution. Such effects become operational at relatively high salt concentrations and are distinct from non-specific electrostatic interactions, known for a long time to lead to salting-in at very low ionic strenghts. As an example, concentrated guanidinium chloride acts as a strong denaturant of model peptides, whereas concentrated guanidinium sulfate does not, This difference arises from the passivation of the denaturating guanidinium cations by appreciable ion pairing with sulfate anions in the solution. Additionally, more specialized ion-binding sites with tailored functional groups and geometries, such as active sites of enzymes or membrane ion channels, are usually considered to be beyond the purview of generic Hofmeister effects. We show, however, that new insights may be gained by extending the realms of Hofmeister chemistry in this direction. Such extensions are possible since there is significant mechanistic overlap between the Hofmeister ion ordering and ion-specific interactions in these specialized ion-binding sites.
 Cremer, P. S.; Jungwirth, P.: Beyond Hofmeister. Nature Chemistry, 6 (2014) 261.
Talk held by:
Pavel Jungwirth. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, 16610 Prague 6, Czech Republic, email@example.com
Further information by:
Prof. Dr. Werner Nau, Professor of Chemistry, Focus Area: Health - Life Sciences & Chemistry - Email: firstname.lastname@example.org, Tel: +49 421 200-3223 - Link to Homepage: http://www.jacobs-university.de/ses/wnau
09/24/2015 Bremer Unternehmertage
Sept. 24-25, 2015
10/01/2015 Falling Walls Lab Bremen 2015
Falling Walls Labs offer bright young researchers, entrepreneurs and professionals the chance to present ground-breaking research projects, initiatives, ideas and business models from all disciplines.
The northern German qualifying Lab for this year’s Falling Walls Lab final will take place at Jacobs University on Thursday, October 1st 2015.
10/14/2015 CoWell Brown Bag Research Seminar
In and beyond ‘differences’ and ‘distance’
10/14/2015 Wie die Windräder aufs Meer kommen
Fenster zur Wissenschaft
10/17/2015 jacobsHack! 2015
JacobsHack! Fall 2015
Jacobs University, Bremen, Germany
"I Hack, Therefore I Am!". Under this slogan the foundation for jacobsHack! was laid when on Feb 1, 2014 the students of Jacobs University met to code for 19 hours on whatever project they considered interesting. On October 4th, 2014 we then took the next step and opened jacobsHack! for external students. In total 85 students from 30 nations participated at jacobsHack! Fall creating one of the most culturally diverse hackathons in Europe.
Visit the website for more information and to apply.
12/09/2015 CoWell Brown Bag Research Seminar
MoLife Research Seminar: Prof. Dr. Andrea Rentmeister
Substrate Promiscuity of Enzymes – A Promising Starting Point for Selective Modification of Biomolecules
Enzymes are usually regarded as highly specific for their natural substrate. However, many, if not most, enzymes can act on substrates other than the ones for which they have evolved. It is therefore interesting to think of non-natural substrates that can be converted as a consequence of substrate promiscuity in order to apply enzymes for our purposes – such as modification of biomolecules. Protein engineering can then be used to shift the substrate scope and obtain enzyme variants with new specificities.
In my talk I will present two different examples of enzyme promiscuity. First, I will talk about a bi-specific adenylation domain of a non-ribosomal peptide synthetase that can selectively activate two out of the 20 standard amino acids. We will look at the structural details to understand this unusual specificity and see how it can be switched by single substitutions. In the second part of my talk, I will show how promiscuity of an RNA methyltransferases can be used to site-specifically label eukaryotic mRNA with fluorescence or affinity tags.
Seminar will be hold by:
Prof. Dr. Andrea Rentmeister, Institut für Biochemie, Westfälische Wilhelms-Universität Münster, Germany
Further information by:
Prof. Dr. Christian Hammann, Professor of Biochemistry - Life Sciences & Chemistry
Building Research II, Room 119, Email: email@example.com, Tel: +49 421 200-3247, Link to Homepage: https://www.jacobs-university.de/ses/chammann/ribogenetics