TY - BOOK A1 - Jeske, Janin A1 - Brehmer, Bastian A1 - Menge, Falko A1 - Hüttenrauch, Stefan A1 - Adam, Christian A1 - Schüler, Benjamin A1 - Schult, Wolfgang A1 - Rasche, Andreas A1 - Polze, Andreas T1 - Aspektorientierte Programmierung : Überblick über Techniken und Werkzeuge T3 - Technische Berichte des Hasso-Plattner-Instituts für Softwaresystemtechnik an der Universität Potsda Y1 - 2006 SN - 3-939469-23-8 SN - 1613-5652 VL - 14 PB - Universitätsverlag Potsdam CY - Potsdam ER - TY - BOOK A1 - Adam, Christian A1 - Brehmer, Bastian A1 - Hüttenrauch, Stefan A1 - Jeske, Janin A1 - Polze, Andreas A1 - Rasche, Andreas A1 - Schüler, Benjamin A1 - Schult, Wolfgang T1 - Aspektorientierte Programmierung : Überblick über Techniken und Werkzeuge N2 - Inhaltsverzeichnis 1 Einführung 2 Aspektorientierte Programmierung 2.1 Ein System als Menge von Eigenschaften 2.2 Aspekte 2.3 Aspektweber 2.4 Vorteile Aspektorientierter Programmierung 2.5 Kategorisierung der Techniken und Werkzeuge f ¨ ur Aspektorientierte Programmierung 3 Techniken und Werkzeuge zur Analyse Aspektorientierter Softwareprogramme 3.1 Virtual Source File 3.2 FEAT 3.3 JQuery 3.4 Aspect Mining Tool 4 Techniken und Werkzeuge zum Entwurf Aspektorientierter Softwareprogramme 4.1 Concern Space Modeling Schema 4.2 Modellierung von Aspekten mit UML 4.3 CoCompose 4.4 Codagen Architect 5 Techniken und Werkzeuge zur Implementierung Aspektorientierter Softwareprogramme 5.1 Statische Aspektweber 5.2 Dynamische Aspektweber 6 Zusammenfassung T3 - Technische Berichte des Hasso-Plattner-Instituts für Digital Engineering an der Universität Potsdam - 14 Y1 - 2006 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-33796 SN - 978-3-939469-23-0 PB - Universitätsverlag Potsdam CY - Potsdam ER - TY - JOUR A1 - Ndah, Hycenth Tim A1 - Schuler, Johannes A1 - Diehl, Katharina A1 - Bateki, Christian A1 - Sieber, Stefan A1 - Knierim, Andrea T1 - From dogmatic views on conservation agriculture adoption in Zambia towards adapting to context JF - International Journal of Agricultural Sustainability N2 - Conservation Agriculture (CA) has been widely promoted in sub-Saharan Africa (SSA) as a sustainable agricultural practice, yet with debatable success. Most authors assume successful adoption, only if all three principles of CA are implemented: (1) minimum or zero tillage, (2) maintenance of a permanent soil cover, and (3) integration of crop rotations. Based on this strict definition, adoption has declined or remained stagnant. Presently, not much attention has been given to context-suited adaptation possibilities, and partial adoption has not been recognized as an entry point to full adoption. Furthermore, isolated success cases have not been analysed sufficiently. By applying the QAToCA approach based on focus group discussions complemented by semi-structured qualitative expert and farmer interviews, we assessed the reasons behind positive CA adaptation and adoption trends in Zambia. Main reasons behind Zambia’s emerging success are (1) a positive institutional influence, (2) a systematic approach towards CA promotion – encouraging a stepwise adaptation and adoption, and (3) mobilization of strong marketing dynamics around CA. These findings could help to eventually adjust or redesign CA promotion activities. We argue for a careful shift from the ‘dogmatic view’ on adoption of CA as a packaged technology, towards adapting its principles to the small-scale farming context of SSA. KW - Conservation agriculture KW - adaptation KW - partial adoption KW - QAToCA KW - Zambia Y1 - 2018 U6 - https://doi.org/10.1080/14735903.2018.1447227 SN - 1473-5903 SN - 1747-762X VL - 16 IS - 2 SP - 228 EP - 242 PB - Routledge, Taylor & Francis Group CY - Abingdon 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 - König, Hannes Jochen A1 - Uthes, Sandra A1 - Schuler, Johannes A1 - Zhen, Lin A1 - Purushothaman, Seema A1 - Suarma, Utia A1 - Sghaier, Mongi A1 - Makokha, Stella A1 - Helming, Katharina A1 - Sieber, Stefan A1 - Chen, Le A1 - Brouwer, Floor A1 - Morris, Jake A1 - Wiggering, Hubert T1 - Regional impact assessment of land use scenarios in developing countries using the FoPIA approach - findings from five case studies JF - Journal of environmental management N2 - The impact of land use changes on sustainable development is of increasing interest in many regions of the world. This study aimed to test the transferability of the Framework for Participatory Impact Assessment (FoPIA), which was originally developed in the European context, to developing countries, in which lack of data often prevents the use of data-driven impact assessment methods. The core aspect of FoPIA is the stakeholder-based assessment of alternative land use scenarios. Scenario impacts on regional sustainability are assessed by using a set of nine regional land use functions (LUFs), which equally cover the economic, social and environmental dimensions of sustainability. The cases analysed in this study include (1) the alternative spatial planning policies around the Merapi volcano and surrounding areas of Yogyakarta City, Indonesia; (2) the large-scale afforestation of agricultural areas to reduce soil erosion in Guyuan, China; (3) the expansion of soil and water conservation measures in the Oum Zessar watershed, Tunisia; (4) the agricultural intensification and the potential for organic agriculture in Bijapur, India; and (5) the land degradation and land conflicts resulting from land division and privatisation in Narok, Kenya. All five regions are characterised by population growth, partially combined with considerable economic development, environmental degradation problems and social conflicts. Implications of the regional scenario impacts as well as methodological aspects are discussed. Overall, FoPIA proved to be a useful tool for diagnosing regional human-environment interactions and for supporting the communication and social learning process among different stakeholder groups. KW - (Ex-ante) impact assessment KW - Land use change KW - Scenario study KW - Sustainable development KW - Stakeholder participation KW - Developing countries KW - Indicators Y1 - 2013 U6 - https://doi.org/10.1016/j.jenvman.2012.10.021 SN - 0301-4797 SN - 1095-8630 VL - 127 SP - S56 EP - S64 PB - Elsevier CY - London ER - TY - JOUR A1 - Schuler, Benjamin A1 - Fürst, Frank A1 - Osterroth, Frank A1 - Steinbacher, Stefan A1 - Huber, Robert A1 - Seckler, Robert T1 - Plasticity and steric strain in a parallel beta-helix: Rational mutations in P22 tailspike protein N2 - By means of genetic screens, a great number of mutations that affect the folding and stability of the tailspike protein from Salmonella phage P22 have been identified. Temperature-sensitive folding (tsf) mutations decrease folding yields at high temperature, but hardly affect thermal stability of the native trimeric structure when assembled at low temperature. Global suppressor (su) mutations mitigate this phenotype. Virtually all of these mutations are located in the central domain of tailspike, a large parallel beta-helix. We modified tailspike by rational single amino acid replacements at three sites in order to investigate the influence of mutations of two types: (1) mutations expected to cause a tsf phenotype by increasing the side-chain volume of a core residue, and (2) mutations in a similar structural context as two of the four known su mutations, which have been suggested to stabilize folding intermediates and the native structure by the release of backbone strain, an effect well known for residues that are primarily evolved for function and not for stability or folding of the protein. Analysis of folding yields, refolding kinetics and thermal denaturation kinetics in vitro show that the tsf phenotype can indeed be produced rationally by increasing the volume of side chains in the beta-helix core. The high-resolution crystal structure of mutant T326F proves that structural rearrangements only take place in the remarkably plastic lumen of the beta-helix, leaving the arrangement of the hydrogen-bonded backbone and thus the surface of the protein unaffected. This supports the notion that changes in the stability of an intermediate, in which the beta-helix domain is largely formed, are the essential mechanism by which tsf mutations affect tailspike folding. A rational design of su mutants, on the other hand, appears to be more difficult. The exchange of two residues in the active site expected to lead to a drastic release of steric strain neither enhanced the folding properties nor the stability of tailspike. Apparently, side-chain interactions in these cases overcompensate for backbone strain, illustrating the extreme optimization of the tailspike protein for conformational stability. The result exemplifies the view arising from the statistical analysis of the distribution of backbone dihedral angles in known three-dimensional protein structures that the adoption of straight phi/psi angles other than the most favorable ones is often caused by side-chain interactions. Y1 - 2000 UR - http://www3.interscience.wiley.com/cgi-bin/abstract/71001984/START ER - TY - JOUR A1 - Miller, Stefan A1 - Schuler, Benjamin A1 - Seckler, Robert T1 - Phages P22 tailspike protein: Removal of head-binding domain unmasks efects of folding mutations on native- state thermal stability Y1 - 1998 ER - TY - JOUR A1 - Miller, Stefan A1 - Schuler, Benjamin A1 - Seckler, Robert T1 - A reversibly unfolding fragment of P22 tailspike protein with native structure : the isolated beta-helix domain Y1 - 1998 ER - TY - CHAP A1 - Scharhag-Rosenberger, Friederike A1 - Carlsohn, Anja A1 - Schüler, Stefan A1 - Lundby, Carsten A1 - Mayer, Frank A1 - Scharhag, Jürgen T1 - Physiological changes over four maximal incremental cycling tests within one day T2 - Medicine and science in sports and exercise : official journal of the American College of Sports Medicine Y1 - 2012 SN - 0195-9131 VL - 44 SP - 933 EP - 934 PB - Lippincott Williams & Wilkins CY - Philadelphia ER -