122 research outputs found

    Demografischer Wandel, alternde Belegschaften und betriebliche Innovation

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    Aktuelle Zahlen der amtlichen Statistik zeigen, dass sich im Zuge des demografischen Wandels die Altersstruktur der Erwerbstätigen in Deutschland in den letzten Jahren verschoben hat. Dieser Trend wird sich in den nächsten zwei Jahrzehnten noch deutlicher fortsetzen. So wird laut Statistischem Bundesamt (2009) der Anteil älterer Beschäftigter in Zukunft deutlich ansteigen. Gleichzeitig werden immer weniger junge Menschen in das Erwerbsleben nachrücken. Richenhagen (2003) spricht – mit Blick auf Deutschland – in diesem Zusammenhang von einer Entwicklung zu alternden Unternehmen“. Es ist davon auszugehen, dass der Altersdurchschnitt der Belegschaften stärker ansteigen wird als der Altersdurchschnitt der Bevölkerung im erwerbsfähigen Alter (Allmendinger & Ebner, 2006; Arlt, Dietz & Walwei, 2009)

    Innovatives Verhalten: ein Geben und Nehmen? : Innovation als Austauschprozess zwischen Mitarbeitern und Unternehmen

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    Innovationen bestimmen die Zukunftsfähigkeit und somit das langfristige Überleben eines Unternehmens. Sie sind die Resultate einer Reihe innovativer Verhaltensweisen verschiedener betrieblicher Akteure. Zur Beantwortung der Frage, wie innovatives Verhalten in Unternehmen zustande kommen, wurde vor dem Hintergrund sozialpsychologischer Ansätze – wie der Ausstauch- und Ressourcentheorie – der Innovationsprozess in der vorliegenden Studie als Tauschgeschäft im Sinne eines Gebens und Nehmens zwischen der Organisation auf der einen und Mitarbeitern auf der anderen Seite verstanden und untersucht. Mit dem Ziel sowohl aus Sicht der Mitarbeiter als auch der des Unternehmens Vorstellungen über mögliche Tauschbeiträge zu identifizieren, wurden teilstrukturierte Interviews mit Betriebsräten, Führungskräften, Innovationsmanagern und Mitarbeitern in sechs verschiedenen Unternehmen aus der Metall- und Elektrobranche durchgeführt

    High-Resolution X-Ray Structure of the Trimeric Scar/WAVE-Complex Precursor Brk1

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    The Scar/WAVE-complex links upstream Rho-GTPase signaling to the activation of the conserved Arp2/3-complex. Scar/WAVE-induced and Arp2/3-complex-mediated actin nucleation is crucial for actin assembly in protruding lamellipodia to drive cell migration. The heteropentameric Scar/WAVE-complex is composed of Scar/WAVE, Abi, Nap, Pir and a small polypeptide Brk1/HSPC300, and recent work suggested that free Brk1 serves as a homooligomeric precursor in the assembly of this complex. Here we characterized the Brk1 trimer from Dictyostelium by analytical ultracentrifugation and gelfiltration. We show for the first time its dissociation at concentrations in the nanomolar range as well as an exchange of subunits within different DdBrk1 containing complexes. Moreover, we determined the three-dimensional structure of DdBrk1 at 1.5 Å resolution by X-ray crystallography. Three chains of DdBrk1 are associated with each other forming a parallel triple coiled-coil bundle. Notably, this structure is highly similar to the heterotrimeric α-helical bundle of HSPC300/WAVE1/Abi2 within the human Scar/WAVE-complex. This finding, together with the fact that Brk1 is collectively sandwiched by the remaining subunits and also constitutes the main subunit connecting the triple-coil domain of the HSPC300/WAVE1/Abi2/ heterotrimer to Sra1(Pir1), implies a critical function of this subunit in the assembly process of the entire Scar/WAVE-complex

    A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation

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    Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules and their complexes, reporting on their size and shape in free solution. The purpose of this multi-laboratory study was to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques. Three kits of AUC cell assemblies containing radial and temperature calibration tools and a bovine serum albumin (BSA) reference sample were shared among 67 laboratories, generating 129 comprehensive data sets. These allowed for an assessment of many parameters of instrument performance, including accuracy of the reported scan time after the start of centrifugation, the accuracy of the temperature calibration, and the accuracy of the radial magnification. The range of sedimentation coefficients obtained for BSA monomer in different instruments and using different optical systems was from 3.655 S to 4.949 S, with a mean and standard deviation of (4.304 ± 0.188) S (4.4%). After the combined application of correction factors derived from the external calibration references for elapsed time, scan velocity, temperature, and radial magnification, the range of s-values was reduced 7-fold with a mean of 4.325 S and a 6-fold reduced standard deviation of ± 0.030 S (0.7%). In addition, the large data set provided an opportunity to determine the instrument-to-instrument variation of the absolute radial positions reported in the scan files, the precision of photometric or refractometric signal magnitudes, and the precision of the calculated apparent molar mass of BSA monomer and the fraction of BSA dimers. These results highlight the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies

    A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation.

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    Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules and their complexes, reporting on their size and shape in free solution. The purpose of this multi-laboratory study was to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques. Three kits of AUC cell assemblies containing radial and temperature calibration tools and a bovine serum albumin (BSA) reference sample were shared among 67 laboratories, generating 129 comprehensive data sets. These allowed for an assessment of many parameters of instrument performance, including accuracy of the reported scan time after the start of centrifugation, the accuracy of the temperature calibration, and the accuracy of the radial magnification. The range of sedimentation coefficients obtained for BSA monomer in different instruments and using different optical systems was from 3.655 S to 4.949 S, with a mean and standard deviation of (4.304 ± 0.188) S (4.4%). After the combined application of correction factors derived from the external calibration references for elapsed time, scan velocity, temperature, and radial magnification, the range of s-values was reduced 7-fold with a mean of 4.325 S and a 6-fold reduced standard deviation of ± 0.030 S (0.7%). In addition, the large data set provided an opportunity to determine the instrument-to-instrument variation of the absolute radial positions reported in the scan files, the precision of photometric or refractometric signal magnitudes, and the precision of the calculated apparent molar mass of BSA monomer and the fraction of BSA dimers. These results highlight the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies
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