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This article compares a selection of recent German literary representations of cycling in the context of contemporary discourses of slow travel, with a particular focus on themes of happiness and emotional authenticity. It seeks to expand the framework of discussions of slow travel with a comparative focus on four novels: Der Mann auf dem Hochrad ('The Man on the Penny Farthing', 1984) by Uwe Timm, Im Sommer wieder Fahrrad ('I'll Cycle Again in the Summer', 2016) by Lea Streisand, Im Feld ('In the Field', 2018) by Joachim Zelter and Neujahr ('New Year', 2018) by Juli Zeh. The article surveys the cultural history of cycling, and pays attention to the status of cycling in German society and culture. Drawing on the work of John Day, Valeria Luiselli, Erling Kagge and Mihaly Csikszentmihalyi, it presents a reading of the texts' treatment of cycling as performance within a broader reflection upon slow travel as a nonfunctional, affective and authentic practice is experienced as a contrast to everyday life. Keywords cylcing, cycling in Germany, cycling in literature, German literature, travel writing, slow travel, Uwe Timm, Lea Streisand, Joachim Zelter, Juli Zeh, history of sport, history of leisure, tourism in literature, emotions in literature, happiness in literature, psychology and literature, This article compares a selection of recent German literary representations of cycling, a form of transport that, I shall argue, deserves a place in contemporary discourses of slow travel. As [...]

Sorghum, a short‐day tropical plant, has been adapted for temperate grain production, in particular through the selection of variants at the MATURITY loci (Ma1–Ma6) that reduce photoperiod sensitivity. Ma3 encodes phytochrome B (phyB), a red/far‐red photochromic biliprotein photoreceptor. The multi‐domain gene product, comprising 1178 amino acids, autocatalytically binds the phytochromobilin chromophore to form the photoactive holophytochrome (Sb.phyB). This study describes the development of an efficient heterologous overproduction system which allows the production of large quantities of various holoprotein constructs, along with purification and crystallization procedures. Crystals of the Pr (red‐light‐absorbing) forms of NPGP, PGP and PG (residues 1–655, 114–655 and 114–458, respectively), each C‐terminally tagged with His6, were successfully produced. While NPGP crystals did not diffract, those of PGP and PG diffracted to 6 and 2.1 Å resolution, respectively. Moving the tag to the N‐terminus and replacing phytochromobilin with phycocyanobilin as the ligand produced PG crystals that diffracted to 1.8 Å resolution. These results demonstrate that the diffraction quality of challenging protein crystals can be improved by removing flexible regions, shifting fusion tags and altering small‐molecule ligands. [ABSTRACT FROM AUTHOR]

Red and far-red light–sensing phytochromes are widespread in nature, occurring in plants, algae, fungi, and prokaryotes. Despite at least a billion years of evolution, their photosensory modules remain structurally and functionally similar. Conversely, nature has found remarkably different ways of transmitting light signals from the photosensor to diverse physiological responses. We summarize key features of phytochrome structure and function and discuss how these are correlated, from how the bilin environment affects the chromophore to how light induces cellular signals. Recent advances in the structural characterization of bacterial and plant phytochromes have resulted in paradigm changes in phytochrome research that we discuss in the context of present-day knowledge. Finally, we highlight questions that remain to be answered and suggest some of the benefits of understanding phytochrome structure and function. [ABSTRACT FROM AUTHOR]

This article comparatively assesses the representation of workers' leisure in Berlin in three significant examples of experimental German cinema from the late Weimar Republic: Mutter Krausens Fahrt ins Glück (Mother Krause's Journey to Happiness, dir. Piel Jutzi, 1929), Menschen am Sonntag (People on Sunday, dir. Robert Siodmak, Edgar G. Ulmer, 1930), and Kuhle Wampe oder Wem gehört die Welt? (Kuhle Wampe or Who Owns the World?, dir. Slatan Dudow, 1932). There are distinct thematic and formal parallels between this set of nearly contemporaneous, generically hybrid films, and the article assesses the inter-related functions of time and space in the films' depiction of leisure experiences in Berlin. Focal points include the depiction of urban space, especially the tenement block and the 'semi-public' space of the courtyard; the Freibad or lakeside bathing resort; the worker sports movement; and the comparative relevance of the work of the Berlin artist Heinrich Zille. The article approaches the films in the historical context of the workers' movement and working-class culture, and is further informed by insights into urban space developed within the sociological discipline of leisure studies. [ABSTRACT FROM AUTHOR]

Both thermally stable states of phytochrome, Pr and Pfr, have been studied by [sup.13]C and [sup.15]N cross-polarization (CP) magic-angle spinning (MAS) NMR using cyanobacterial (Cphl) and plant (phyA) phytochrome sensory modules containing uniformly [sup.13]C and [sup.15]N-labeled bilin chromophores. Two-dimensional homo- and heteronudear experiments allowed most of the [sup.13]C chemical shifts to be assigned in both states. Chemical shift differences reflect changes of the electronic structure of the cofactor at the atomic level as well as its interactions with the chromophore-binding pocket. The chromophore in cyanobacterial and plant phytochromes shows very similar features in the respective Pr and Pfr states. The data are interpreted in terms of a strengthened hydrogen bond at the ring D carbonyl. The red shift in the Pfr state is explained by the increasing length of the conjugation network beyond ring C including the entire ring D. Enhanced conjugation within the [pi]-osystem stabilizes the more tensed chromophore in the Pfr state. Concomitant changes at the ring C propionate carboxylate and the ring D carbonyl are explained by a loss of hydrogen bonding to Cph1-His-290 and transmittance of conformational changes to the ring C propionate via a water network. These and other conformational changes may lead to modified surface interactions, e.g., along the tongue region contacting the bilin chromophore. photornorphogenesis | photoreceptors | chromophore-protein interaction phycocyanobilin | solid-state NMR

The chief executive officer (CEO) and board of directors of ExxonMobil, known as Esso in the U.K., made a determined effort between 1998 and 2004 to mislead and deceive the world by conveying a false impression about the truth of climate change. ExxonMobil employed a strategy of disinformation, similar to the campaign used by tobacco firms since the mid-1950s, to create uncertainty over the scientific consensus on global warming.

The transition of Synechocystis PCC 6803 phytochrome Cph1 and its N-terrminal sensor domain from Pr to Pfr leads to net proton release, which is a function of proton release from decay of an intermediate and of proton uptake associated with Pfr formation. Protons arise from ionizable amino acid side chains.

The complete sequence of the Synechocystis chromosome has revealed a phytochrome-like sequence that yielded an authentic phytochrome when overexpressed in Escherichia coli. In this paper we describe this recombinant Synechocystis phytochrome in more detail. Islands of strong similarity to plant phytochromes were found throughout the cyanobacterial sequence whereas C-terminal homologies identify it as a likely sensory histidine kinase, a family to which plant phytochromes are related. An [approximately equal to] 300 residue portion that is important for plant phytochrome function is missing from the Synechocystis sequence, immediately in front of the putative kinase region. The recombinant apoprotein is soluble and can easily be purified to homogeneity by affinity chromatography. Phycocyanobilin and similar tetrapyrroles are covalently attached within seconds, an autocatalytic process followed by slow conformational changes culminating in red-absorbing phytochrome formation. Spectral absorbance characteristics are remarkably similar to those of plant phytochromes, although the conformation of the chromophore is likely to be more helical in the Synechocystis phytochrome. According to size-exclusion chromatography the native recombinant apoproteins and holoproteins elute predominantly as 115- and 170-kDa species, respectively. Both tend to form dimers in vitro and aggregate under low salt conditions. Nevertheless, the purity and solubility of the recombinant gene product make it a most attractive model for molecular studies of phytochrome, including x-ray crystallography.

Raman spectroscopy and nanosecond flash photolysis were used to study a recombinant phytochrome of the cyanobacterium Synechocystis. The findings indicate a resemblance between recombinant Synechocystis phytochrome and plant phytochrome with regard to Raman and visible spectral properties of the Pr and Pfr states. However, although the Synechocystis phytochrome undergoes a photoreversible conversion, red-shifted intermediates with kinetics different from those determined for the phytochrome intermediates were observed.