BANKING REFORM BY STATUTE

The lamentable failure of our banking system to function satisfactorily in the performance of its duties to the public raises at the outset two kinds of questions. Is there something fundamentally unsound about the structure of our banking machinery or does the trouble reside merely in a lack of understanding on the part of bankers of the proper management of the detailed activities in which banks necessarily engage? Or may the unsatisfactory result be ascribed to a combination of these two alternatives? The position taken in this paper is that the structure of our banking system is inherently unsound and that far too large a proportion of bankers have no conception of the fundamental principles of sound banking. When we turn our attention to possible remedies for these defects we are at once confronted not only with the problem of what changes might be efficacious, but also with the question as to the power of the federal government to prescribe by statute the necessary alterations for other than national banks

High-mobility Hydrogenated Indium Oxide without Introducing Water During Sputtering

AbstractThe key role of water to obtain high-mobility IO:H (hydrogenated indium oxide) layers has been well documented, but introducing the required tiny amount of water is technologically challenging. We first use simulations to evidence the key role of high mobility for the transparent conductive oxide for high-efficiency crystalline silicon solar cells. Then, we investigate an approach to fabricate high-mobility IO:H that circumvent the introduction of water vapor, relying on water vapor from ambient air. A sputtering tool equipped with a residual gas analyzer allows partial pressure monitoring of hydrogen and water in the system, and to link the gas composition to the properties of the deposited films. To vary the residual water pressure, we varied the pumping time after opening the chamber and before starting the deposition to reach different base pressures (1. 10-5 mbar to 3. 10-7 mbar), which are mostly composed of residual water. An optimum base pressure around 3. 10-6 mbar—and not lower pressures—was found to yield the highest mobility values after annealing. An alternative approach by introducing a small flow of hydrogen together with argon and oxygen is also shown to provide promising results

Characterization of the stimulation of SNARE-mediated membrane fusion by the SM protein Munc18a

The mammalian neuronal Sec1p/Munc18 protein Muncl8a binds tightly to the t-SNARE Syntaxin1a in isolation, and the binary Muncl8a/Syntaxin1a interaction is thought to prevent formation of the Syntaxin1a/SNAP25b t-SNARE complex required for intracellular membrane fusion. However, both Sec1p and Munc18a are required factors for exocytosis and stimulate in vitro membrane fusion of the appropriate preassembled t-SNARE complex and v-SNARE. The experiments presented here show that Muncl8a stimulates the initial rate and final extent of membrane fusion driven by the neuronal t-SNAREs Syntaxin1a/SNAP25b and v-SNARE VAMP2 and elucidate the molecular mechanism underlying the increase in membrane fusion. Munc18a binds to the assembled neuronal t-SNARE complex in a functional manner much like its yeast homolog Sec1p. The Munc18a/t-SNARE complex interaction appears to occur through Syntaxin1a but not SNAP25b because Munc18a stimulates fusion of a Syntaxin1a/yeast Sec9c t-SNARE complex and fails to interact with yeast SNAREs. Munc18a displays a well-characterized interaction with the Syntaxin1a N-terminal regulatory domain (NRD), but also contacts the Syntaxin1a SNARE Core Complex (H3) domain to stimulate fusion because fusion of a yeast t-SNARE complex chimera in which the yeast Sso1p NRD was replaced with the Syntaxin1a NRD was not stimulated by Munc18a. Deletion of a flexible linker region between the Syntaxin1a NRD and H3 domain that permits movement of the NRD abolishes the ability of Munc18a to stimulate membrane fusion, suggesting that Munc1a may actively position the Syntaxin1a NRD to favor membrane fusion. In addition, Munc18a directly and functionally interacts with VAMP2. Taken together, these results suggest strongly that Munc18a acts as a scaffold that increases the efficiency of t-SNARE complex and v-SNARE interactions, resulting in accelerated membrane fusion. Furthermore, Munc18a may also function in combination with the calcium sensor Synaptotagmin I to enhance neurosecretion at the last stage of exocytosis