106 research outputs found

    Assembly and Test of a Support Structure for 3.6 m Long Nb3Sn Racetrack Coils”,

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    Abstract-The LHC Accelerator Research Program (LARP) is currently developing 4 m long Nb 3 Sn quadrupole magnets for a possible upgrade of the LHC Interaction Regions (IR). In order to provide a reliable test bed for the fabrication and test of long Nb 3 Sn coils, LARP has started the development of the long racetrack magnet LRS01. The magnet is composed of two 3.6 m long racetrack coils contained in a support structure based on an aluminum shell pre-tensioned with water-pressurized bladders and interference keys. For the phase-one test of the assembly procedure and loading operation, the structure was pre-stressed at room temperature and cooled down to 77 K with instrumented, solid aluminum "dummy coils". Mechanical behavior and stress homogeneity were monitored with strain gauges mounted on the shell and the dummy coils. The dummy coils were replaced with reacted and impregnated Nb 3 Sn coils in a second assembly procedure, followed by cool-down to 4.5 K and powered magnet test. This paper report on the assembly and loading procedures of the support structure as well as the comparison between strain gauge data and 3D model predictions

    Multiscale Simulations Suggest a Mechanism for the Association of the Dok7 PH Domain with PIP-Containing Membranes

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    Dok7 is a peripheral membrane protein that is associated with the MuSK receptor tyrosine kinase. Formation of the Dok7/MuSK/membrane complex is required for the activation of MuSK. This is a key step in the complex exchange of signals between neuron and muscle, which lead to neuromuscular junction formation, dysfunction of which is associated with congenital myasthenic syndromes. The Dok7 structure consists of a Pleckstrin Homology (PH) domain and a Phosphotyrosine Binding (PTB) domain. The mechanism of the Dok7 association with the membrane remains largely unknown. Using multi-scale molecular dynamics simulations we have explored the formation of the Dok7 PH/membrane complex. Our simulations indicate that the PH domain of Dok7 associates with membranes containing phosphatidylinositol phosphates (PIPs) via interactions of the β1/β2, β3/β4, and β5/β6 loops, which together form a positively charged surface on the PH domain and interact with the negatively charged headgroups of PIP molecules. The initial encounter of the Dok7 PH domain is followed by formation of additional interactions with the lipid bilayer, and especially with PIP molecules, which stabilizes the Dok7 PH/membrane complex. We have quantified the binding of the PH domain to the model bilayers by calculating a density landscape for protein/membrane interactions. Detailed analysis of the PH/PIP interactions reveal both a canonical and an atypical site to be occupied by the anionic lipid. PH domain binding leads to local clustering of PIP molecules in the bilayer. Association of the Dok7 PH domain with PIP lipids is therefore seen as a key step in localization of Dok7 to the membrane and formation of a complex with MuSK

    Insulin signalling and the regulation of glucose and lipid metabolism

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    The epidemic of type 2 diabetes and impaired glucose tolerance is one of the main causes of morbidity and mortality worldwide. In both disorders, tissues such as muscle, fat and liver become less responsive or resistant to insulin. This state is also linked to other common health problems, such as obesity, polycystic ovarian disease, hyperlipidaemia, hypertension and atherosclerosis. The pathophysiology of insulin resistance involves a complex network of signalling pathways, activated by the insulin receptor, which regulates intermediary metabolism and its organization in cells. But recent studies have shown that numerous other hormones and signalling events attenuate insulin action, and are important in type 2 diabetes.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/62568/1/414799a.pd

    A Study of the Electrodeposition of Ruthenium from Very Dilute Solutions

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