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Inhalt:
- Eberhard Knobloch und Ingo Schwarz: Alexander von Humboldt und Hector Berlioz
- Oliver Lubrich: „[M]on extrême répugnance à écrire la relation de mon voyage“ – Alejandro de Humboldt deconstruye la relación de viaje
- Eva-Maria Siegel: Repräsentation und Augenschein. Organisation des Wissens und Wahrnehmung des Fremden um 1800 am Beispiel der Reiseberichte und -tagebücher Alexander von Humboldts
- Engelhard Weigl: Acclimatization: The Schomburgk brothers in South Australia
Inhalt:
- Ursula Thiemer-Sachse: El “Museo histórico indiano” de Lorenzo Boturini Benaduci y los esfuerzos del erudito alemán Alejandro de Humboldt para preservar sus restos para una interpretación científica
- Ursula Thiemer-Sachse: Petroglifos en rocas de la Cordillera de la Costa así como en los raudales de los ríos de la selva virgen venezolana. La interpretación por Alejandro de Humboldt y observaciones actuales
- Ingo Schwarz: „Ein beschränkter Verstandesmensch ohne Einbildungskraft“ – Anmerkungen zu Friedrich Schillers Urteil über Alexander von Humboldt
- Michael Zeuske: Humboldteanización del mundo occidental? La importancia del viaje de Humboldt para Europa y América Latina
De processibus matrimonialibus : Fachzeitschrift zu Fragen des kanonischen Ehe- und Prozeßrechtes
(2003)
The Parody of "Parody as Cultural Memory" in Richard Powers" Galatea 2.2 : a response to Anca Rosu
(2003)
Man möchte meinen, die Zeit für Religion sei gekommen, da die grossen Gegenentwürfe wie Kommunismus und Psychoanalyse abgedankt haben. Aber an die Stelle klarer Alternativen tritt zunehmend das unbeschwerte Spiel der Sinnmöglichkeiten. Das Christentum wird zu einer Möglichkeit unter anderen. Deshalb steht das Christentum in einer pluralen Gesellschaft unter besonderem Profilierungsdruck. Man will wissen, wozu es dient und worin der Beitrag der Christen für die moderne Gesellschaft besteht. Das Elixier moderner Pluralität ist der Individualismus. Er besteht wesentlich in der Möglichkeit, an Traditionen nicht anzuknüpfen. Menschen sind immer weniger bereit, Totalentwürfe zu übernehmen, welche die ganze Existenz umfassen. Wie verträglich ist dann eine freie Gesinnungsgemeinschaft im Kontext pluraler Nachbarschaft? Welchen Stellenwert besitzt Religion in öffentlichen Räumen wie Schule und Medien? Welche Rolle spielen die Gläubigen angesichts der Vielfalt von Modellen und Vorbildern?
Die Klosterkirche der Benediktinerabtei Ottobeuren ist eines der Hauptwerke des europäischen Barock. Die CD-ROM bietet Besuchern und einem kunsthistorisch interessiertem Publikum eine einzigartige Präsentation und völlig neue Perspektiven. Im Barockzeitalter kombinierten die Künstler bei der Innenausstattung von Kirchen, gezielt ölbilder, Stuck und Fresken mit der Architektur zu umfassenden theologischen Gesamtkunstwerken. Hinter dem Gewimmel aus Heiligen, Allegorien, Engeln und Reliquiaren vermag der kundig geführte Betrachter vielerlei Bezüge zu entdecken. Die CD-ROM gibt Antwort auf Fragen die sich jeder Besucher eines barocken Kirchenraumes schon einmal gestellt haben dürfte. Weshalb liegen in den Schausärgen Skelette? Warum stürzen Teufel aus dem Bild? Wozu mahnen die unterschiedlichen Tugenden? Aus dem Inhalt: · Vollständige digitale Rekonstruktion einer der berühmtesten Kirchen des europäischen Barock · ca. 500 hochauflösende Bilder sowie Kamerafahrten, 1300 Textseiten · über 70 Fachtheologen, Kunsthistoriker, Seelsorger, Lehrer und Studierende aus Deutschland, österreich und den USA interpretieren den Innenraum der Basilika Ottobeuren. Der verlinkte Himmel - ein Kirchenbesuch der besonderen Art!
Der Blick auf die Weichenstellungen der Christentumsgeschichte dient dazu, sich angesichts konkurrierender Religiositäten des eigenen Profils zu vergewissern. Eine solche zentrale Weiche ist die Entwicklung im 2. Jahrhundert, weil in dieser Zeit Kanon, Ämter, Theologie ausdifferenziert wurden. Wie das Christentum sich in dieser Zeit zu einem selbstdefinierten und fortsetzungsfähigen System entwickelte, lässt sich mit dem Instrumentarium aus Luhmanns Religionstheorie ueberzeugend darstellen.
Gernig, K. (Hrsg.); Nacktheit. Ästhetische Inszenierungen im Kulturvergleich; Köln, Böhlau, 2002
(2003)
The paper seeks to analyse the case of the theologian Tinius, one of the best-known representatives of >book- addiction< (bibliomania), as it is described in authentic contemporary documents, popular literature and fictionalised adaptations. Explanations of the phenomenon range from a special socialisation, rational calculation, criminal anthropology, and the >Faustian urge for knowledge<, to diabolical bibliophily and a theology of sin. A historical synopsis shows the heterogeneity of the contemporary criminal and psychiatric discourse on bibliomania as a >literary disease<. The continuing reception of the bibliomania exemplified by Tinius in a variety of literary genres suggests that it incorporates a considerable amount of >social energy<, based on the fascination with the >Other< of reason.
In order to investigate the behavior of single molecules under conditions far from equilibrium, we have coupled a microfabricated laminar-flow mixer to a confocal optical system. This combination enables time-resolved measurement of Foerster resonance energy transfer after an abrupt change in solution conditions. Observations of a small protein show the evolution of the intramolecular distance distribution as folding progresses. This technique can expose subpopulations, such as unfolded protein under conditions favoring the native structure, that would be obscured in equilibrium experiments.
The fructose-1,6-bis(phosphate) aldolase isologous tetramer tightly associates through two different subunit interfaces defined by its 222 symmetry. Both single- and double-interfacial mutant aldolases have a destabilized quaternary structure, but there is little effect on the catalytic activity. These enzymes are however thermolabile. This study demonstrates the temperature-dependent dissociation of the mutant enzymes and determines the dissociation free energies of both mutant and native aldolase. Subunit dissociation is measured by sedimentation equilibrium in the analytical ultracentrifuge. At 25C the tetramerdimer dissociation constants for each single-mutant enzyme are similar, about 10 -6 M. For the double-mutant enzyme, sedimentation velocity experiments on sucrose density gradients support a tetramermonomer equilibrium. Furthermore, sedimentation equilibrium experiments determined a dissociation constant of 10- 15 M3 for the double-mutant enzyme. By the same methods the upper limit for the dissociation constant of wild-type aldolase A is approximately 10-28 M3, which indicates an extremely stable tetramer. The thermodynamic values describing monomer-tetramer and dimer-tetramer equilibria are analyzed with regard to possible cooperative interaction between the two subunit interfaces.
Summary Using five different steps, ;-Galactosidase has been purified from kidney beans to apparent electrophoretic homogeniety with approximately 90-fold purificationwith a specific activity of 281 units mg;1 protein. A single bandwas observed in native PAGE. Activity staining of the native gel with 5-bromo4-chloro 3-indoxyl ;-D-galactopyranoside (X-Gal) at pH 4.0 also produceda single band. Analytical gel filtration in Superdex G-75 revealed the molecularmass of the native protein to be approximately 75 kD. 10 percnt; SDS-PAGE under reducingconditions showed two subunits of molecular masses, 45 and 30 kD, respectively.Hence, ;-galactosidase from kidney beans is a heterodimer. A typical proteinprofile with ;max at 280 nm was observed and A280/A260ratio was 1.52. The N-terminal sequence of the 45 kD band showed 86 percnt; sequencehomology with an Arabidopsis thaliana and 85 percnt; with Lycopersiconesculentum putative ;-galactosidase sequences. The Electrospray MassSpectrometric analysis of this band also revealed a peptide fragment that had90 percnt; sequence homology with an Arabidopsis thaliana putative ;- galactosidasesequence. The N-terminal sequencing of the 30 kD band as well as mass spectrometricanalysis both by MALDI- TOF and ES MS revealed certain sequences that matchedwith phytohemagglutinin of kidney beans. The optimum pH of the enzyme was 4.0and it hydrolysed o- and p-nitrophenyl ;-D galactopyranosidewith a Km value of 0.63 mmol/L and 0.74 mmol/L, respectively.The energy of activation calculated from the Arrhenius equation was 14.8 kcal/molenzyme site. The enzyme was found to be comparatively thermostable showing maximumactivity at 67 °C. Thermal denaturation of the enzyme at 65 °C obeyssingle exponential decay with first order-rate constant 0.105 min;1.Galactose, a hydrolytic product of this enzyme was a competitive inhibitor witha Ki of 2.7 mmol/L.
Bacteriophage Sf6 tailspike protein is functionally equivalent to the well characterized tailspike ofSalmonella phage P22, mediating attachment of the viral particle to host cell-surface polysaccharide. However, there is significant sequence similarity between the two 70-kDa polypeptides only in the N-terminal putative capsid-binding domains. The major, central part of P22 tailspike protein, which forms a parallel ;-helix and is responsible for saccharide binding and hydrolysis, lacks detectable sequence homology to the Sf6 protein. After recombinant expression in Escherichia coli as a soluble protein, the Sf6 protein was purified to homogeneity. As shown by circular dichroism and Fourier transform infrared spectroscopy, the secondary structure contents of Sf6 and P22 tailspike proteins are very similar. Both tailspikes are thermostable homotrimers and resist denaturation by SDS at room temperature. The specific endorhamnosidase activities of Sf6 tailspike protein toward fluorescence-labeled dodeca-, deca-, and octasaccharide fragments of Shigella O-antigen suggest a similar active site topology of both proteins. Upon deletion of the N-terminal putative capsid-binding domain, the protein still forms a thermostable, SDS-resistant trimer that has been crystallized. The observations strongly suggest that the tailspike of phage Sf6 is a trimeric parallel ;-helix protein with high structural similarity to its functional homolog from phage P22.
Small-subunit (SSU) rRNA genes (rDNA) were amplified by PCR from a hot pool environmental DNA sample using Bacteria- or Archaea-specific rDNA primers. Unique rDNA types were identified by restriction fragment length polymorphism (RFLP) analysis and representative sequences were determined. Family 10 glycoside hydrolase consensus PCR primers were used to explore the occurrence and diversity of xylanase genes in the hot pool environmental DNA sample. Partial sequences for three different xylanases were obtained and genomic walking PCR (GWPCR), in combination with nested primer pairs, was used to obtained a unique 1,741-bp nucleotide sequence. Analysis of this sequence identified a putative XynA protein encoded by the xynA open reading frame. The single module novel xylanase shared sequence similarity to the family 10 glycoside hydrolases. The purified recombinant enzyme, XynA expressed in E. coli exhibited optimum activity at 100 degrees C and pH 6.0, and was extremely thermostable at 90 degrees C. The enzyme showed high specificity toward different xylans and xylooligosaccharides.