111 research outputs found
A Step-based framework to combine creativity, project management, and technical development in industrial innovation
No full textA step-based framework to combine creativity, project management and technical development in industrial innovation
No full textMolecular dynamics simulation of a functional fragment of Myelin Basic Protein in membrane and effects of post-translational modifications
No full textSupporting product innovation in uncertainuty conditions: a UsDSP based decision making approach
No full textA systematic innovation case study: new concepts of domestic appliance drying cycle
No full textWhile incremental innovation is for most companies a well assessed
process, radical product innovation is often handled with difficulty, mainly due to
myriad obstacles in the idea-to cash process which limits company’s ability to
innovate. As a typical approach, engineers firstly try to find innovative solutions
only inside their technological product space, basically thinking accordingly to
their commonly assessed know-how. In this paper an industrial case is analyzed,
showing how TRIZ methodology offers to technicians a systematic way to solve
problematic contradictions and find effective ideas
Strategies for Efficient Exploitation of Solar Energy: A Model of the Photovoltaic Conversion Process Based on TRIZ, the Theory of Inventive Problem Solving
No full textWhile PV has been developing dramatically in the last few years, the scope for improving energy conversion remains enormous, as witnessed by gap between the efficiency of commercial products (10-20%) and a theoretical potential for reaching over 60%. In this context it is important to be able to horizon-scan for new and improved concepts in a systematic and structured way. The Theory of Inventive Problem Solving (also known as TRIZ) has been applied to analyse the PV conversion process, taking a c-Si cell as the baseline scenario. Comparison of several innovative concepts with this baseline highlights their potential impact on loss mechanisms. The approach has the potential to provide important insights for future PV technology innovation, although further work is needed
Impaired placental vascularization and embryo growth after in-vitro manipulation in sheep: a morphometric study
No full textIntroduction. Aberrant placentation occurs early during embryonic development after assisted reproductive techniques. To further understand this failure, vascular morphometry of ovine placentas and embryo growth after in vitro activation (IVA) and in vitro fertilization (IVF) at 20 and 22 days of gestation was performed.Results. Crown-ramp measure (mm) after in vitro manipulation is reduced at 20 (CTR-controls: 3.84; IVF: 3.48; IVA: 3.46) and 22 days (CTR: 4.42; IVF: 3.84; IVA: 3.74), as well as placental vessel number/field (20-22 days: IVF: 1.25-1.93; IVA: 1.24-1.71; CTR: 3.11-3.48). At 20 d, stage 1 vessels (early vasculogenesis) were prevalent in IVA samples (IVA: 26.67% of total vessels; IVF: 10.55%; CTR: 3.54%), stage 2 (early tube formation) in IVF (IVF: 77.82%; CTR: 70.31%; IVA: 66.33%) and stage 3 (late vasculogenesis) in CTR (CTR: 26.15%; IVF: 11.63%; IVA: 10%). At 22 d, more vessels in stages 1 (18.18%) and 2 (72.72%) occur after IVA than IVF (1: 5.24%; 2: 64.51%) and CTR (1: 2.62%; 2: 53.59%), while CTR had more stage 3 vessels (43.79%) than IVF (30.25%) and IVA (9.1%). Discussion. In vitro manipulation leads to delayed maturation and reduced density of placental vessels, that affect post-implantation embryo growth. [...
Binding of the proline-rich segment of Myelin Basic Protein to SH3-domains – spectroscopic, microarray and modelling studies of ligand conformation and effects of post-translational modifications
No full textMyelin basic protein (MBP) is a multifunctional protein involved in maintaining the stability and integrity of the myelin sheath by a variety of interactions with membranes and with cytoskeletal and other proteins. A central segment of MBP is highly conserved in mammals and consists of a membrane surface-associated amphipathic -helix, immediately followed by a proline-rich segment that we hypothesize is an SH3 ligand. We show by circular dichroic spectroscopy that this proline-rich segment forms a polyproline type II helix in vitro under physiological conditions and that phosphorylation at a constituent threonyl residue has a stabilizing effect on its conformation. Using SH3 domain microarrays, we observe that the unmodified recombinant murine 18.5 kDa MBP isoform (rmC1 component) binds the following SH3 domains: Yes1 > PSD95 > cortactin = PexD = Abl = Fyn = c-Src = Itk in order of decreasing affinity. A quasi-deiminated form of the protein (rmC8) binds the SH3 domains Yes1 > Fyn > cortactin = c-Src > PexD = Abl. Phosphorylation of rmC1 at 1-2 threonines within the proline-rich segment by mitogen-activated protein kinase in vitro has no effect on the binding specificity to the SH3 domains on the array. An SH3 domain of chicken Fyn is also demonstrated to bind to lipid membrane-associated C1, phosphorylated C1, and rmC8. Molecular docking simulations of the interaction of the putative SH3 ligand of classic MBP with the human Fyn SH3 domain indicate that the strength of the interaction is of the same order of magnitude as with calmodulin and that the molecular recognition and association is mediated by some weak CH··· interactions between the ligand prolyl residues and the aromatic ones of the SH3 binding site. One such interaction is well-conserved and involves the stacking of an MBP-peptide prolyl and an SH3 domain tryptophanyl residue, as in most other SH3-ligand complexes. Lysyl and arginyl residues in the peptide canonically interact via salt bridges and cation- interactions with negatively charged and aromatic residues in the SH3 domain binding site. Posttranslational modifications (phosphorylation or methylation) of the ligand cause noticeable shifts in the conformation of the flexible peptide and its side chains but do not predict any major inhibition of the binding beyond somewhat less favorable interactions for peptides with phosphorylated seryl or threonyl residues
Characterization of the acidic infolding intermediate of bovine Odorant Binding Protein: a spectroscopic and computational approach
No full textConformational choreography of a molecular switch region in myelin basic protein—Molecular dynamics shows induced folding and secondary structure type conversion upon threonyl phosphorylation in both aqueous and membrane-associated environments
No full textAbstractThe 18.5kDa isoform of myelin basic protein is essential to maintaining the close apposition of myelin membranes in central nervous system myelin, but its intrinsic disorder (conformational dependence on environment), a variety of post-translational modifications, and a diversity of protein ligands (e.g., actin and tubulin) all indicate it to be multifunctional. We have performed molecular dynamics simulations of a conserved central segment of 18.5kDa myelin basic protein (residues Glu80–Gly103, murine sequence numbering) in aqueous and membrane-associated environments to ascertain the stability of constituent secondary structure elements (α-helix from Glu80–Val91 and extended poly-proline type II from Thr92–Gly103) and the effects of phosphorylation of residues Thr92 and Thr95, individually and together. In aqueous solution, all four forms of the peptide bent in the middle to form a hydrophobic cluster. The phosphorylated variants were stabilized further by electrostatic interactions and formation of β-structures, in agreement with previous spectroscopic data. In simulations performed with the peptide in association with a dimyristoylphosphatidylcholine bilayer, the amphipathic α-helical segment remained stable and membrane-associated, although the degree of penetration was less in the phosphorylated variants, and the tilt of the α-helix with respect to the plane of the membrane also changed significantly with the modifications. The extended segment adjacent to this α-helix represents a putative SH3-ligand and remained exposed to the cytoplasm (and thus accessible to binding partners). The results of these simulations demonstrate how this segment of the protein can act as a molecular switch: an amphipathic α-helical segment of the protein is membrane-associated and presents a subsequent proline-rich segment to the cytoplasm for interaction with other proteins. Phosphorylation of threonyl residues alters the degree of membrane penetration of the α-helix and the accessibility of the proline-rich ligand and can stabilize a β-bend. A bend in this region of 18.5kDa myelin basic protein suggests that the N- and C-termini of the proteins can interact with different leaflets of the myelin membrane and explain how a single protein can bring them close together
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