TY - BOOK A1 - Hofmann, Robert A1 - Bauerle, David A1 - Hofmann, Robert A1 - Kolls, Ronja T1 - Zur Quelle : Magazin von und für Zaubernde Y1 - 2013 PB - Univ. CY - Potsdam ER - TY - CHAP A1 - Borowski, Andreas A1 - Glowinski, Ingrid A1 - Frister, Jonas A1 - Höttecke, Dietmar A1 - Buth, Katrin A1 - Koenen, Jenna A1 - Masanek, Nicole A1 - Reichwein, Wilko A1 - Scholten, Nina A1 - Sprenger, Sandra A1 - Stender, Peter A1 - Wöhlke, Carina A1 - Komorek, Michael A1 - Freckmann, Janine A1 - Hofmann, Josefine A1 - Niesel, Verena A1 - Richter, Chris A1 - Mehlmann, Nelli A1 - Bikner-Ahsbahs, Angelika A1 - Unverricht, Katja A1 - Schanze, Sascha A1 - Bittorf, Robert Marten A1 - Meier, Monique A1 - Grospietsch, Finja A1 - Mayer, Jürgen A1 - Gimbel, Katharina A1 - Ziepprecht, Kathrin A1 - Hofmann, Judith A1 - Kramer, Charlotte A1 - Müller, Britta-Kornelia A1 - Rohde, Andreas A1 - Zühlsdorf, Felix A1 - Winkler, Iris A1 - Laging, Ralf A1 - Peter, Carina A1 - Schween, Michael A1 - Härle, Gerhard A1 - Busse, Beatrix A1 - Mahner, Sebastian A1 - Köstler, Verena A1 - Kufner, Sabrina A1 - Mägdefrau, Jutta A1 - Müller, Christian A1 - Beck, Christina A1 - Kriehuber, Eva A1 - Boch, Florian A1 - Engl, Anna-Teresa A1 - Helzel, Andreas A1 - Pickert, Tina A1 - Reiter, Christian A1 - Blasini, Bettina A1 - Nerdel, Claudia A1 - Lewalter, Doris A1 - Schiffhauer, Silke A1 - Richter-Gebert, Jürgen A1 - Bannert, Maria A1 - Maahs, Mirjam A1 - Reißner, Maria A1 - Ungar, Patrizia A1 - von Wachter, Jana-Kristin A1 - Hellmann, Katharina A1 - Zaki, Katja A1 - Pohlenz, Philipp ED - Glowinski, Ingrid ED - Borowski, Andreas ED - Gillen, Julia ED - Schanze, Sascha ED - von Meien, Joachim T1 - Kohärenz in der universitären Lehrerbildung T1 - Coherence in teacher education at university BT - Vernetzung von Fachwissenschaft, Fachdidaktik und Bildungswissenschaften BT - linking studies in content knowledge, pedagogical content knowledge and pedagogical knowledge in teacher education N2 - One area that is supported by the project “Qualitätsoffensive 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. N2 - Eine verbesserte Zusammenarbeit und Abstimmung von Fachwissenschaft, Fachdidaktik, Bildungswissenschaften und schulpraktischen Lernorten ist einer der Förderbereiche der „Qualitätsoffensive Lehrerbildung“. Zahlreiche der geförderten Projekte haben für dieses Handlungsfeld im Bereich Vernetzung von Fachwissenschaft, Fachdidaktik und Bildungswissenschaften hochschulspezifische Maßnahmen konzipiert und umgesetzt. Der vorliegende Tagungsband beinhaltet Beiträge von 15 entsprechenden Projekten, von denen sieben anlässlich von zwei standortübergreifenden Projekt-Tagungen in Hannover und Potsdam vorgestellt und in Workshops diskutiert wurden. Insgesamt geben die Beiträge einen theoretisch fundierten und gleichzeitig praxisorientierten Überblick über aktuelle Ansätze und Konzepte zur besseren Vernetzung fachwissenschaftlicher, fachdidaktischer und bildungswissenschaftlicher Studienanteile im Lehramtsstudium. Dargestellt werden Projektarbeiten der Hochschulen, die auf verschiedenen Ebenen wirksam werden (curricular-inhaltliche Ebene, kollegiale Ebene, hochschul-strukturelle Ebene). Die Maßnahmen sind so beschrieben, dass sie als Grundlage für einen Transfer auf andere Fächer bzw. andere Standorte genutzt werden können. Die Beiträge richten sich an alle Lehrenden im Bereich der Lehramtsbildung sowie sonstige Akteure im Bereich der Lehr- und Qualitätsentwicklung an den Universitäten. Sie alle können den beschriebenen Konzepten und Umsetzungsformaten transferierbare Ideen und Impulse entnehmen. KW - Professionswissen KW - universitäre Lehrerbildung KW - Vernetzung Fachwissenschaft KW - Fachdidaktik KW - Bildungswissenschaft KW - Lehramtsstudium KW - teacher education KW - professional knowledge KW - content knowledge KW - pedagogical content knowledge Y1 - 2018 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-414267 SN - 978-3-86956-438-8 PB - Universitätsverlag Potsdam CY - Potsdam ER - TY - GEN A1 - Best, Robert B. A1 - Zheng, Wenwei A1 - Borgia, Alessandro A1 - Buholzer, Karin A1 - Borgia, Madeleine B. A1 - Hofmann, Hagen A1 - Soranno, Andrea A1 - Nettels, Daniel A1 - Gast, Klaus A1 - Grishaev, Alexander A1 - Schuler, Benjamin T1 - Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water" T2 - Science N2 - 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. Y1 - 2018 U6 - https://doi.org/10.1126/science.aar7101 SN - 0036-8075 SN - 1095-9203 VL - 361 IS - 6405 PB - American Assoc. for the Advancement of Science CY - Washington ER - TY - JOUR A1 - Nettels, Daniel A1 - Müller-Späth, Sonja A1 - Küster, Frank A1 - Hofmann, Hagen A1 - Haenni, Domminik A1 - Rüegger, Stefan A1 - Reymond, Luc A1 - Hoffmann, Armin S. A1 - Kubelka, Jan A1 - Heinz, Benjamin A1 - Gast, Klaus A1 - Best, Robert B. A1 - Schuler, Benjamin T1 - Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins N2 - 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. Y1 - 2009 UR - http://www.pnas.org/content/106/49/20740.full.pdf+html SN - 0027-8424 ER - TY - JOUR A1 - Borgia, Alessandro A1 - Zheng, Wenwei A1 - Buholzer, Karin A1 - Borgia, Madeleine B. A1 - Schüler, Anja A1 - Hofmann, Hagen A1 - Soranno, Andrea A1 - Nettels, Daniel A1 - Gast, Klaus A1 - Grishaev, Alexander A1 - Best, Robert B. A1 - Schuler, Benjamin T1 - Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods JF - Journal of the American Chemical Society N2 - 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. Y1 - 2016 U6 - https://doi.org/10.1021/jacs.6b05917 SN - 0002-7863 VL - 138 SP - 11714 EP - 11726 PB - American Chemical Society CY - Washington ER - TY - JOUR A1 - Soergel, Bjoern A1 - Kriegler, Elmar A1 - Weindl, Isabelle A1 - Rauner, Sebastian A1 - Dirnaichner, Alois A1 - Ruhe, Constantin A1 - Hofmann, Matthias A1 - Bauer, Nico A1 - Bertram, Christoph A1 - Bodirsky, Benjamin Leon A1 - Leimbach, Marian A1 - Leininger, Julia A1 - Levesque, Antoine A1 - Luderer, Gunnar A1 - Pehl, Michaja A1 - Wingens, Christopher A1 - Baumstark, Lavinia A1 - Beier, Felicitas A1 - Dietrich, Jan Philipp A1 - Humpenöder, Florian A1 - von Jeetze, Patrick A1 - Klein, David A1 - Koch, Johannes A1 - Pietzcker, Robert C. A1 - Strefler, Jessica A1 - Lotze-Campen, Hermann A1 - Popp, Alexander T1 - A sustainable development pathway for climate action within the UN 2030 Agenda JF - Nature climate change N2 - 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. KW - climate-change mitigation KW - climate-change policy KW - socioeconomic scenarios KW - sustainability Y1 - 2021 U6 - https://doi.org/10.1038/s41558-021-01098-3 SN - 1758-678X SN - 1758-6798 VL - 11 IS - 8 SP - 656 EP - 664 PB - Nature Publishing Group CY - London ER -