Fournier, G, Hinderer H, Schmid D, Seign R, Baumann M.
2012.
The new mobility paradigm: Transformation of value chain and business models. Enterprise and Work Innovation Studies. 8:9-40.
AbstractFour 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.
Morgado, L, Fernandes AP, Dantas JM, Silva MA, Salgueiro CA.
2012.
On the road to improve the bioremediation and electricity-harvesting skills of Geobacter sulfurreducens: functional and structural characterization of multihaem cytochromes. Biochemical Society transactions. 40(6):1295-1301.
AbstractExtracellular electron transfer is one of the physiological hallmarks of Geobacter sulfurreducens, allowing these bacteria to reduce toxic and/or radioactive metals and grow on electrode surfaces. Aiming to functionally optimize the respiratory electron-transfer chains, such properties can be explored through genetically engineered strains. Geobacter species comprise a large number of different multihaem c-type cytochromes involved in the extracellular electron-transfer pathways. The functional characterization of multihaem proteins is particularly complex because of the coexistence of several microstates in solution, connecting the fully reduced and oxidized states. NMR spectroscopy has been used to monitor the stepwise oxidation of each individual haem and thus to obtain information on each microstate. For the structural study of these proteins, a cost-effective isotopic labelling of the protein polypeptide chains was combined with the comparative analysis of 1H-13C HSQC (heteronuclear single-quantum correlation) NMR spectra obtained for labelled and unlabelled samples. These new methodological approaches allowed us to study G. sulfurreducens haem proteins functionally and structurally, revealing functional mechanisms and key residues involved in their electron-transfer capabilities. Such advances can now be applied to the design of engineered haem proteins to improve the bioremediation and electricity-harvesting skills of G. sulfurreducens.
Cândido, AC.
2012.
Open Innovation and Social Network Analysis. Enterprise and Work Innovation Studies. 8:41-55.
AbstractIn this work we propose the use of Social Network Analysis to understand the positioning of the concept of Open Innovation in the literature, offering thereby a complementary approach to existing literature review up to now. The main motivation of this network analysis is to contribute to the understanding of the concept of Open Innovation, with its spread to different areas of knowledge over the years and its relationship with other concepts in the literature. Some 403 articles published in the database of the Science Direct during the years 2003 to 2011 were analyzed. The data was collected separately by year, considering the following information: journals in which the articles were published; countries of origin of the articles’ authors, keywords of these articles and year of publication. The results reveal the intense growth of the use of the words "Open Innovation" in articles from different areas of knowledge, as well as its increasing interconnection with other concepts, allowing the understanding of its diffusion in the literature.
Dantas, JM, Morgado L, Londer YY, Fernandes AP, Louro RO, Pokkuluri PR, Schiffer M, Salgueiro CA.
2012.
Pivotal role of the strictly conserved aromatic residue F15 in the cytochrome c7 family. Journal of Biological Inorganic Chemistry. 17(1):11-24.
AbstractCytochromes c7 are periplasmic triheme proteins that have been reported exclusively in δ-proteobacteria. The structures of five triheme cytochromes identified in Geobacter sulfurreducens and one in Desulfuromonas acetoxidans have been determined. In addition to the hemes and axial histidines, a single aromatic residue is conserved in all these proteins - phenylalanine 15 (F15). PpcA is a member of the G. sulfurreducens cytochrome c7 family that performs electron/proton energy transduction in addition to electron transfer that leads to the reduction of extracellular electron acceptors. For the first time we probed the role of the F15 residue in the PpcA functional mechanism, by replacing this residue with the aliphatic leucine by site-directed mutagenesis. The analysis of NMR spectra of both oxidized and reduced forms showed that the heme core and the overall fold of the mutated protein were not affected. However, the analysis of 1H-15N heteronuclear single quantum coherence NMR spectra evidenced local rearrangements in the α-helix placed between hemes I and III that lead to structural readjustments in the orientation of heme axial ligands. The detailed thermodynamic characterization of F15L mutant revealed that the reduction potentials are more negative and the redox-Bohr effect is decreased. The redox potential of heme III is most affected. It is of interest that the mutation in F15, located between hemes I and III in PpcA, changes the characteristics of the two hemes differently. Altogether, these modifications disrupt the balance of the global network of cooperativities, preventing the F15L mutant protein from performing a concerted electron/proton transfer.
Batalha, IL, Lowe CR, Roque ACA.
2012.
Platforms for enrichment of phosphorylated proteins and peptides in proteomics. Trends in Biotechnology. 30(2):100-110.
AbstractProtein 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.
Kuckova, S, et al.
2012.
Protein identification and localization using mass spectrometry and staining tests in cross-sections of polychrome samples. Journal of Cultural Heritage.
AbstractThe identification and localization of the proteinaceous binders are essential issues in studies of painting materials and techniques, for further proposing valid restoration and conservation treatments of the painted or polychrome works of art. The challenge for analytical chemists and conservation scientists is the availability of methods able to simultaneously identify and map the presence of the binders in the multilayered structure of a sample and the possibility to use a very low amount of sample from the studied art object (considering also the criteria of minimum sampling). These methods should be fast, reproducible in different artefacts and in case of mixture of protein-based binders with other non-proteinaceous constituents (oils, resins, waxes, gums etc.) and also economical (both in terms of materials and time consume). In this context, the present paper proposes an innovative protocol of investigation using two complementary techniques – Matrix-Assisted Laser Desorption/Ionisation – Time of Flight Mass Spectrometry (MALDI-TOF MS) and staining tests (one visible and one fluorescent stain) assisted by Optical Microscopy (OM) on cross-section of samples – for the simultaneous identification and mapping of protein – and oil-based binders in paint materials. The novelty is based on the use of MALDI-TOF MS on cross-sections of paints together with a fluorescent stain for protein identification and mapping (mainly used in the area of proteomics) complementing the use of a traditional visible stain for oil-based material identification. The protocol was successfully applied on several samples taken from a Czech medieval polychrome sculpture, entitled “The Mourning of Jesus Christ” (16th century) belonging to the Moravian Gallery (Brno).
Simão, J, Veiga L.
2012.
QoE-JVM: An Adaptive and Resource-Aware Java Runtime for Cloud Computing. On the Move to Meaningful Internet Systems: OTM 2012. 7566:566-583.: Springer Berlin / Heidelberg
AbstractCloud computing has been dominated by system-level virtual machines to enable the management of resources using a coarse grained approach, largely in a manner independent from the applications running on these infrastructures. However, in such environments, although different types of applications can be running, the resources are often delivered in a equal manner to each one, missing the opportunity to manage the available resources in a more efficient and application aware or driven way. Our proposal is QoE-JVM supporting Java applications with a global and elastic distributed image of a high-level virtual machine (HLLVM), where total resource consumption and allocation (within and across applications in the infrastructure) are driven by incremental gains in quality-of-execution (QoE), which relates the resources allocated to an application and the performance the application can extract from having those resources. In this paper, we discuss how critical resources (memory and CPU) can be allocated among HLL-VMs, so that Cloud providers can exchange resource slices among virtual machines, continually adaptdressing where those resources are required, while being able to determine where the reduction will be more economically effective, i.e., will contribute in lesser extent to performance degradation.
Morgado, L, Paixão VB, Schiffer M, Pokkuluri PR, Bruix M, Salgueiro CA.
2012.
Revealing the structural origin of the redox-Bohr effect: the first solution structure of a cytochrome from Geobacter sulfurreducens. Biochemical Journal. 441(1):179-187.
AbstractGs (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.
Fonseca, BM, Paquete CM, Salgueiro CA, Louro RO.
2012.
The role of intramolecular interactions in the functional control of multiheme cytochromes c. FEBS Lett. 586(5):504-509.
AbstractDetailed thermodynamic and structural data measured in soluble monomeric multiheme cytochromes c provided the basis to investigate the functional significance of interactions between redox co-factors. The steep decay of intramolecular interactions with distance means that close proximity of the redox centers is necessary to modulate the intrinsic reduction potentials in a significant way. This ensures selection of specific populations during redox activity in addition to maintaining fast intramolecular electron transfer. Therefore, intramolecular interactions between redox co-factors play an important role in establishing the biological function of the protein by controlling how electrons flow through and are distributed among the co-factors.