@book{JeskeBrehmerMengeetal.2006, author = {Jeske, Janin and Brehmer, Bastian and Menge, Falko and H{\"u}ttenrauch, Stefan and Adam, Christian and Sch{\"u}ler, Benjamin and Schult, Wolfgang and Rasche, Andreas and Polze, Andreas}, title = {Aspektorientierte Programmierung : {\"U}berblick {\"u}ber Techniken und Werkzeuge}, series = {Technische Berichte des Hasso-Plattner-Instituts f{\"u}r Softwaresystemtechnik an der Universit{\"a}t Potsda}, volume = {14}, journal = {Technische Berichte des Hasso-Plattner-Instituts f{\"u}r Softwaresystemtechnik an der Universit{\"a}t Potsda}, publisher = {Universit{\"a}tsverlag Potsdam}, address = {Potsdam}, isbn = {3-939469-23-8}, issn = {1613-5652}, pages = {88 S.}, year = {2006}, language = {de} } @book{AdamBrehmerHuettenrauchetal.2006, author = {Adam, Christian and Brehmer, Bastian and H{\"u}ttenrauch, Stefan and Jeske, Janin and Polze, Andreas and Rasche, Andreas and Sch{\"u}ler, Benjamin and Schult, Wolfgang}, title = {Aspektorientierte Programmierung : {\"U}berblick {\"u}ber Techniken und Werkzeuge}, publisher = {Universit{\"a}tsverlag Potsdam}, address = {Potsdam}, isbn = {978-3-939469-23-0}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-33796}, publisher = {Universit{\"a}t Potsdam}, pages = {88}, year = {2006}, abstract = {Inhaltsverzeichnis 1 Einf{\"u}hrung 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 ยจ 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}, language = {de} } @article{NdahSchulerDiehletal.2018, author = {Ndah, Hycenth Tim and Schuler, Johannes and Diehl, Katharina and Bateki, Christian and Sieber, Stefan and Knierim, Andrea}, title = {From dogmatic views on conservation agriculture adoption in Zambia towards adapting to context}, series = {International Journal of Agricultural Sustainability}, volume = {16}, journal = {International Journal of Agricultural Sustainability}, number = {2}, publisher = {Routledge, Taylor \& Francis Group}, address = {Abingdon}, issn = {1473-5903}, doi = {10.1080/14735903.2018.1447227}, pages = {228 -- 242}, year = {2018}, abstract = {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.}, 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{KoenigUthesSchuleretal.2013, author = {K{\"o}nig, Hannes Jochen and Uthes, Sandra and Schuler, Johannes and Zhen, Lin and Purushothaman, Seema and Suarma, Utia and Sghaier, Mongi and Makokha, Stella and Helming, Katharina and Sieber, Stefan and Chen, Le and Brouwer, Floor and Morris, Jake and Wiggering, Hubert}, title = {Regional impact assessment of land use scenarios in developing countries using the FoPIA approach - findings from five case studies}, series = {Journal of environmental management}, volume = {127}, journal = {Journal of environmental management}, publisher = {Elsevier}, address = {London}, issn = {0301-4797}, doi = {10.1016/j.jenvman.2012.10.021}, pages = {S56 -- S64}, year = {2013}, abstract = {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.}, language = {en} } @article{SchulerFuerstOsterrothetal.2000, author = {Schuler, Benjamin and F{\"u}rst, Frank and Osterroth, Frank and Steinbacher, Stefan and Huber, Robert and Seckler, Robert}, title = {Plasticity and steric strain in a parallel beta-helix: Rational mutations in P22 tailspike protein}, year = {2000}, abstract = {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.}, language = {en} } @article{MillerSchulerSeckler1998, author = {Miller, Stefan and Schuler, Benjamin and Seckler, Robert}, title = {Phages P22 tailspike protein: Removal of head-binding domain unmasks efects of folding mutations on native- state thermal stability}, year = {1998}, language = {en} } @article{MillerSchulerSeckler1998, author = {Miller, Stefan and Schuler, Benjamin and Seckler, Robert}, title = {A reversibly unfolding fragment of P22 tailspike protein with native structure : the isolated beta-helix domain}, year = {1998}, language = {en} } @inproceedings{ScharhagRosenbergerCarlsohnSchueleretal.2012, author = {Scharhag-Rosenberger, Friederike and Carlsohn, Anja and Sch{\"u}ler, Stefan and Lundby, Carsten and Mayer, Frank and Scharhag, J{\"u}rgen}, title = {Physiological changes over four maximal incremental cycling tests within one day}, series = {Medicine and science in sports and exercise : official journal of the American College of Sports Medicine}, volume = {44}, booktitle = {Medicine and science in sports and exercise : official journal of the American College of Sports Medicine}, publisher = {Lippincott Williams \& Wilkins}, address = {Philadelphia}, issn = {0195-9131}, pages = {933 -- 934}, year = {2012}, language = {en} }