Four categories of innovations have been identified by Freeman and Perez: incremental innovations, radical innovations, new technological systems (systemic innovations), and technological revolutions or new techno-economic paradigms. New techno-economic paradigms represent changes in technological systems that are so far-reaching in their effects that they have a major influence on the behaviour of the entire economy. Scarcity of oil and external costs like global warming are the key arguments and the main drivers of the change of the current paradigm. They will affect especially the mobility of individuals and the interlinked business models. Novel business models within newly created markets will raise e.g. extended mobility services, activities aiming at the infrastructure, new opportunities in the field of energy transmission and supply and even new strategies of recycling, reusing or reducing the use of resources in order to address global scarcity issues. Especially for the established players of the automotive industry like original equipment manufacturers (OEMs) or 1st and 2nd tier suppliers this implicates opportunities and risks at the same time. But also new players will get the chance to create and enter new markets with new or extended products or services and lead the new value chain. This paper compiles and evaluates current approaches and business models of selected OEMs together with upcoming players. Additionally their positions within the existing value chain are being analyzed and classified. Bringing together the identified drivers of changes with current trends within the automotive industry the authors also show new concepts of extended business models, e.g. the idea of an ecosystem, that have the potential to cause an additional shift of power within the global mobility value chain.

Protein phosphorylation is a complex and highly dynamic process involved in numerous biological events. Abnormal phosphorylation is one of the underlying mechanisms for the development of cancer and metabolic disorders. The identification and absolute quantification of specific phospho-signatures can help elucidate protein functions in signaling pathways and facilitate the development of new and personalized diagnostic and therapeutic tools. This review presents a variety of strategies currently utilized for the enrichment of phosphorylated proteins and peptides before mass spectrometry analysis during proteomic studies. The investigation of specific affinity reagents, allied to the integration of different enrichment processes, is triggering the development of more selective, rapid and cost-effective high-throughput automated platforms.

Gs (Geobacter sulfurreducens) can transfer electrons to the exterior of its cells, a property that makes it a preferential candidate for the development of biotechnological applications. Its genome encodes over 100 cytochromes and, despite their abundance and key functional roles, to date there is no structural information for these proteins in solution. The trihaem cytochrome PpcA might have a crucial role in the conversion of electronic energy into protonmotive force, a fundamental step for ATP synthesis in the presence of extracellular electron acceptors. In the present study, 15N-labelled PpcA was produced and NMR spectroscopy was used to determine its solution structure in the fully reduced state, its backbone dynamics and the pH-dependent conformational changes. The structure obtained is well defined, with an average pairwise rmsd (root mean square deviation) of 0.25 Å (1 Å=0.1 nm) for the backbone atoms and 0.99 Å for all heavy atoms, and constitutes the first solution structure of a Gs cytochrome. The redox-Bohr centre responsible for controlling the electron/proton transfer was identified, as well as the putative interacting regions between PpcA and its redox partners. The solution structure of PpcA will constitute the foundation for studies aimed at mapping out in detail these interacting regions.

Affinity chromatography with protein A from Staphylococcus aureus (SpA) is the most widespread and
accepted methodology for antibody capture during the downstream process of antibody manufacturing.
A triazine based ligand (ligand 22/8) was previously developed as an inexpensive and robust alternative
to SpA chromatography (Li et al. [12] and Teng et al. [11]). Despite the experimental success, there is no
structural information on the binding modes of ligand 22/8 to antibodies, namely to Immunoglobulin G
(IgG) molecules and fragments. In this work, we addressed this issue by a molecular docking approach
allied to molecular dynamics simulations. Theoretical results confirmed the preference of the synthetic
ligand to bind IgG through the binding site found in the crystallographic structure of the natural complex
between SpA and the Fc fragment of IgG. Our studies also suggested other unknown “hot-spots” for
specific binding of the affinity ligand at the hinge between VH and CH1 domains of Fab fragment. The best
docking poses were further analysed by molecular dynamics studies at three different protonation states
(pH 3, 7 and 11). The main interactions between ligand 22/8 and the IgG fragments found at pH 7 were
weaker at pH 3 and pH 11 and in these conditions the ligand start losing tight contact with the binding
site, corroborating the experimental evidence for protein elution from the chromatographic adsorbents
at these pH conditions.