A Mathematical and Experimental Investigation of the Application of Air Spring to Shock Testing Machines

The applications of many modern devices require them to be able to perform their functions satisfactorily after having been subjected to transient accelerations of considerable magnitude. Some Devices are required to operate even during the period of acceleration. Since failure of components or sub-assemblies during the actual operation of the entire assembly would in general be extremely undesirable and costly (for example, failure of instrumentation in a high-speed aircraft or guided missile might lead to loss of the entire vehicle), it is necessary to test the components and sub-assemblies in order to determine whether they may be exposed to accelerations equivalent to those to which they will be subjected when used in their intended application

The Psychology of Intelligence Analysis: Drivers of Prediction Accuracy in World Politics

This article extends psychological methods and concepts into a domain that is as profoundly consequential as it is poorly understood: intelligence analysis. We report findings from a geopolitical forecasting tournament that assessed the accuracy of more than 150,000 forecasts of 743 participants on 199 events occurring over 2 years. Participants were above average in intelligence and political knowledge relative to the general population. Individual differences in performance emerged, and forecasting skills were surprisingly consistent over time. Key predictors were (a) dispositional variables of cognitive ability, political knowledge, and open-mindedness; (b) situational variables of training in probabilistic reasoning and participation in collaborative teams that shared information and discussed rationales (Mellers, Ungar, et al., 2014); and (c) behavioral variables of deliberation time and frequency of belief updating. We developed a profile of the best forecasters; they were better at inductive reasoning, pattern detection, cognitive flexibility, and open-mindedness. They had greater understanding of geopolitics, training in probabilistic reasoning, and opportunities to succeed in cognitively enriched team environments. Last but not least, they viewed forecasting as a skill that required deliberate practice, sustained effort, and constant monitoring of current affairs

Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex

<p>Abstract</p> <p>Background</p> <p>To study the organization and interaction with the fusion domain (or fusion peptide, FP) of the transmembrane domain (TMD) of influenza virus envelope glycoprotein for its role in membrane fusion which is also essential in the cellular trafficking of biomolecules and sperm-egg fusion.</p> <p>Results</p> <p>The fluorescence and gel electrophoresis experiments revealed a tight self-assembly of TMD in the model membrane. A weak but non-random interaction between TMD and FP in the membrane was found. In the complex, the central TMD oligomer was packed by FP in an antiparallel fashion. FP insertion into the membrane was altered by binding to TMD. An infrared study exhibited an enhanced membrane perturbation by the complex formation. A model was built to illustrate the role of TMD in the late stages of influenza virus-mediated membrane fusion reaction.</p> <p>Conclusion</p> <p>The TMD oligomer anchors the fusion protein in the membrane with minimal destabilization to the membrane. Upon associating with FP, the complex exerts a synergistic effect on the membrane perturbation. This effect is likely to contribute to the complete membrane fusion during the late phase of fusion protein-induced fusion cascade. The results presented in the work characterize the nature of the interaction of TMD with the membrane and TMD in a complex with FP in the steps leading to pore initiation and dilation during virus-induced fusion. Our data and proposed fusion model highlight the key role of TMD-FP interaction and have implications on the fusion reaction mediated by other type I viral fusion proteins. Understanding the molecular mechanism of membrane fusion may assist in the design of anti-viral drugs.</p

Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex

<p>Abstract</p> <p>Background</p> <p>To study the organization and interaction with the fusion domain (or fusion peptide, FP) of the transmembrane domain (TMD) of influenza virus envelope glycoprotein for its role in membrane fusion which is also essential in the cellular trafficking of biomolecules and sperm-egg fusion.</p> <p>Results</p> <p>The fluorescence and gel electrophoresis experiments revealed a tight self-assembly of TMD in the model membrane. A weak but non-random interaction between TMD and FP in the membrane was found. In the complex, the central TMD oligomer was packed by FP in an antiparallel fashion. FP insertion into the membrane was altered by binding to TMD. An infrared study exhibited an enhanced membrane perturbation by the complex formation. A model was built to illustrate the role of TMD in the late stages of influenza virus-mediated membrane fusion reaction.</p> <p>Conclusion</p> <p>The TMD oligomer anchors the fusion protein in the membrane with minimal destabilization to the membrane. Upon associating with FP, the complex exerts a synergistic effect on the membrane perturbation. This effect is likely to contribute to the complete membrane fusion during the late phase of fusion protein-induced fusion cascade. The results presented in the work characterize the nature of the interaction of TMD with the membrane and TMD in a complex with FP in the steps leading to pore initiation and dilation during virus-induced fusion. Our data and proposed fusion model highlight the key role of TMD-FP interaction and have implications on the fusion reaction mediated by other type I viral fusion proteins. Understanding the molecular mechanism of membrane fusion may assist in the design of anti-viral drugs.</p