@book{HofmannBauerleHofmannetal.2013, author = {Hofmann, Robert and Bauerle, David and Hofmann, Robert and Kolls, Ronja}, title = {Zur Quelle : Magazin von und f{\"u}r Zaubernde}, publisher = {Univ.}, address = {Potsdam}, year = {2013}, language = {de} } @inproceedings{BorowskiGlowinskiFristeretal.2018, author = {Borowski, Andreas and Glowinski, Ingrid and Frister, Jonas and H{\"o}ttecke, Dietmar and Buth, Katrin and Koenen, Jenna and Masanek, Nicole and Reichwein, Wilko and Scholten, Nina and Sprenger, Sandra and Stender, Peter and W{\"o}hlke, Carina and Komorek, Michael and Freckmann, Janine and Hofmann, Josefine and Niesel, Verena and Richter, Chris and Mehlmann, Nelli and Bikner-Ahsbahs, Angelika and Unverricht, Katja and Schanze, Sascha and Bittorf, Robert Marten and Meier, Monique and Grospietsch, Finja and Mayer, J{\"u}rgen and Gimbel, Katharina and Ziepprecht, Kathrin and Hofmann, Judith and Kramer, Charlotte and M{\"u}ller, Britta-Kornelia and Rohde, Andreas and Z{\"u}hlsdorf, Felix and Winkler, Iris and Laging, Ralf and Peter, Carina and Schween, Michael and H{\"a}rle, Gerhard and Busse, Beatrix and Mahner, Sebastian and K{\"o}stler, Verena and Kufner, Sabrina and M{\"a}gdefrau, Jutta and M{\"u}ller, Christian and Beck, Christina and Kriehuber, Eva and Boch, Florian and Engl, Anna-Teresa and Helzel, Andreas and Pickert, Tina and Reiter, Christian and Blasini, Bettina and Nerdel, Claudia and Lewalter, Doris and Schiffhauer, Silke and Richter-Gebert, J{\"u}rgen and Bannert, Maria and Maahs, Mirjam and Reißner, Maria and Ungar, Patrizia and von Wachter, Jana-Kristin and Hellmann, Katharina and Zaki, Katja and Pohlenz, Philipp}, title = {Koh{\"a}renz in der universit{\"a}ren Lehrerbildung}, editor = {Glowinski, Ingrid and Borowski, Andreas and Gillen, Julia and Schanze, Sascha and von Meien, Joachim}, publisher = {Universit{\"a}tsverlag Potsdam}, address = {Potsdam}, isbn = {978-3-86956-438-8}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-414267}, year = {2018}, abstract = {One area that is supported by the project "Qualit{\"a}tsoffensive Lehrerbildung" (funded by BMBF) is the improvement of collaboration and coordination between studies in the discipline, studies in pedagogical content knowledge, and studies in pedagogical knowledge during teacher education at university. Aiming a better coordination among these three parts of teacher education at university, many of the supported projects have designed and realized university-specific approaches. This conference proceedings volume comprises contributions by 15 of these projects. Seven of those were introduced and discussed in workshops on the occasion of two cross-regional project-conferences in Hannover and Potsdam. Overall, the contributions give a theoretically funded as well as a practice-oriented overview of current approaches and concepts to achieve a better connection between study units concerning studies in content knowledge, pedagogical content knowledge and pedagogical knowledge in teacher education. The volume presents university projects, which take effect on different levels (at the level of curriculum and content, at a collegiate level, at the level of structural conditions of universities). The different approaches are described in a way that they can provide a basis for transfer to other subjects or further universities. The contributions are aimed at teacher educators as well as other actors working in the field of teaching- and quality development at universities. All of them can take transferable ideas and impulses from the described concepts and formats.}, language = {de} } @misc{BestZhengBorgiaetal.2018, author = {Best, Robert B. and Zheng, Wenwei and Borgia, Alessandro and Buholzer, Karin and Borgia, Madeleine B. and Hofmann, Hagen and Soranno, Andrea and Nettels, Daniel and Gast, Klaus and Grishaev, Alexander and Schuler, Benjamin}, title = {Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"}, series = {Science}, volume = {361}, journal = {Science}, number = {6405}, publisher = {American Assoc. for the Advancement of Science}, address = {Washington}, issn = {0036-8075}, doi = {10.1126/science.aar7101}, pages = {2}, year = {2018}, abstract = {Riback et al. (Reports, 13 October 2017, p. 238) used small-angle x-ray scattering (SAXS) experiments to infer a degree of compaction for unfolded proteins in water versus chemical denaturant that is highly consistent with the results from Forster resonance energy transfer (FRET) experiments. There is thus no "contradiction" between the two methods, nor evidence to support their claim that commonly used FRET fluorophores cause protein compaction.}, language = {en} } @article{NettelsMuellerSpaethKuesteretal.2009, author = {Nettels, Daniel and M{\"u}ller-Sp{\"a}th, Sonja and K{\"u}ster, Frank and Hofmann, Hagen and Haenni, Domminik and R{\"u}egger, Stefan and Reymond, Luc and Hoffmann, Armin S. and Kubelka, Jan and Heinz, Benjamin and Gast, Klaus and Best, Robert B. and Schuler, Benjamin}, title = {Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins}, issn = {0027-8424}, year = {2009}, abstract = {We used single-molecule FRET in combination with other biophysical methods and molecular simulations to investigate the effect of temperature on the dimensions of unfolded proteins. With singlemolecule FRET, this question can be addressed even under nearnative conditions, where most molecules are folded, allowing us to probe a wide range of denaturant concentrations and temperatures. We find a compaction of the unfolded state of a small cold shock protein with increasing temperature in both the presence and the absence of denaturant, with good agreement between the results from single-molecule FRET and dynamic light scattering. Although dissociation of denaturant from the polypeptide chain with increasing temperature accounts for part of the compaction, the results indicate an important role for additional temperaturedependent interactions within the unfolded chain. The observation of a collapse of a similar extent in the extremely hydrophilic, intrinsically disordered protein prothymosin suggests that the hydrophobic effect is not the sole source of the underlying interactions. Circular dichroism spectroscopy and replica exchange molecular dynamics simulations in explicit water show changes in secondary structure content with increasing temperature and suggest a contribution of intramolecular hydrogen bonding to unfolded state collapse.}, language = {en} } @article{BorgiaZhengBuholzeretal.2016, author = {Borgia, Alessandro and Zheng, Wenwei and Buholzer, Karin and Borgia, Madeleine B. and Sch{\"u}ler, Anja and Hofmann, Hagen and Soranno, Andrea and Nettels, Daniel and Gast, Klaus and Grishaev, Alexander and Best, Robert B. and Schuler, Benjamin}, title = {Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods}, series = {Journal of the American Chemical Society}, volume = {138}, journal = {Journal of the American Chemical Society}, publisher = {American Chemical Society}, address = {Washington}, issn = {0002-7863}, doi = {10.1021/jacs.6b05917}, pages = {11714 -- 11726}, year = {2016}, abstract = {There has been a long-standing controversy regarding the effect of chemical denaturants on the dimensions of unfolded and intrinsically disordered proteins: A wide range of experimental techniques suggest that polypeptide chains expand with increasing denaturant concentration, but several studies using small-angle X-ray scattering (SAXS) have reported no: such increase of the radius of gyration (R-g). This inconsistency challenges our current understanding of the mechanism of chemical denaturants, which are widely employed to investigate protein folding and stability. Here, we use a combination Of single-molecule Forster resonance energy transfer (FRET), SAXS, dynamic light scattering (DLS), and two-focus fluorescence correlation spectroscopy (2f-FCS) to characterize the denaturant dependence of the unfolded state of the spectrin domain R17 and the intrinsically disordered protein ACTR in two different denaturants. Standard analysis of the primary data clearly indicates an expansion of the unfolded state with increasing denaturant concentration irrespective of the protein, denaturant, or experimental method used. This is the first case in which SAXS and FRET have yielded even qualitatively consistent results regarding expansion in denaturant when applied to the same proteins. To more directly illustrate this self-consistency, we used both SAXS and FRET data in a Bayesian procedure to refine structural ensembles representative of the observed unfolded state. This analysis demonstrates that both of these experimental probes are compatible with a common ensemble of protein configurations for each denaturant concentration. Furthermore, the resulting ensembles reproduce the trend of increasing hydrodynamic radius, with denaturant concentration obtained by 2f-FCS,and DLS. We were thus able to reconcile the results from all four experimental techniques quantitatively, to obtain a comprehensive structural picture of denaturant;induced unfolded state expansion, and to identify the Most likely sources of earlier discrepancies.}, language = {en} } @article{SoergelKrieglerWeindletal.2021, author = {Soergel, Bjoern and Kriegler, Elmar and Weindl, Isabelle and Rauner, Sebastian and Dirnaichner, Alois and Ruhe, Constantin and Hofmann, Matthias and Bauer, Nico and Bertram, Christoph and Bodirsky, Benjamin Leon and Leimbach, Marian and Leininger, Julia and Levesque, Antoine and Luderer, Gunnar and Pehl, Michaja and Wingens, Christopher and Baumstark, Lavinia and Beier, Felicitas and Dietrich, Jan Philipp and Humpen{\"o}der, Florian and von Jeetze, Patrick and Klein, David and Koch, Johannes and Pietzcker, Robert C. and Strefler, Jessica and Lotze-Campen, Hermann and Popp, Alexander}, title = {A sustainable development pathway for climate action within the UN 2030 Agenda}, series = {Nature climate change}, volume = {11}, journal = {Nature climate change}, number = {8}, publisher = {Nature Publishing Group}, address = {London}, issn = {1758-678X}, doi = {10.1038/s41558-021-01098-3}, pages = {656 -- 664}, year = {2021}, abstract = {Ambitious climate policies, as well as economic development, education, technological progress and less resource-intensive lifestyles, are crucial elements for progress towards the UN Sustainable Development Goals (SDGs). However, using an integrated modelling framework covering 56 indicators or proxies across all 17 SDGs, we show that they are insufficient to reach the targets. An additional sustainable development package, including international climate finance, progressive redistribution of carbon pricing revenues, sufficient and healthy nutrition and improved access to modern energy, enables a more comprehensive sustainable development pathway. We quantify climate and SDG outcomes, showing that these interventions substantially boost progress towards many aspects of the UN Agenda 2030 and simultaneously facilitate reaching ambitious climate targets. Nonetheless, several important gaps remain; for example, with respect to the eradication of extreme poverty (180 million people remaining in 2030). These gaps can be closed by 2050 for many SDGs while also respecting the 1.5 °C target and several other planetary boundaries.}, language = {en} }