The creep of zirconium in water from 400° to 600°F /

"Contract AT-30-1-Gen-366.""Date Declassified: November 29, 1955"--Page [2]."Sylvania Electric Products, Inc.""Subject category: Metallurgy and Ceramics.""April 20, 1951.""SEP-54."Includes bibliographical references (page 17).Mode of access: Internet.This bibliographic record is available under the Creative Commons CC0 "No Rights Reserved" license. The University of Florida Libraries, as creator of this bibliographic record, has waived all rights to it worldwide under copyright law, including all related and neighboring rights, to the extent allowed by law

Drones, Morality, and Vulnerability: Two Arguments Against Automated Killing

This chapter articulates and discusses several arguments against the lethal use of unmanned aerial vehicles, often called drones. A distinction is made between targeted killing, killing at a distance, and automated killing, which is used to map the arguments against lethal drones. After considering issues concerning the justification of war, the argument that targeted killing makes it easier to start a war, and the argument that killing at a distance is problematic, this chapter focuses on two arguments against automated killing, which are relevant to all kinds of “machine killing”. The first argument (from moral agency) questions if machines can ever be moral agents and is based on differences in capacities for moral decision-making between humans and machines. The second argument (from moral patiency), which has received far less attention in the literature on machine ethics and ethics of drones, focuses on the question if machines can ever be “moral patients”. It is argued that there is a morally significant qualitative difference in vulnerability and way of being between drones and humans, and that because of this asymmetry fully automated killing without or with little human involvement is not justified

Globalization, security and drones

No abstract availabl

A molecular mechanism of direction switching in the flagellar motor of Escherichia coli

The direction of flagellar rotation is regulated by a rotor-mounted protein assembly, termed the “switch complex,” formed from multiple copies of the proteins FliG, FliM, and FliN. The structures of major parts of these proteins are known, and the overall organization of proteins in the complex has been elucidated previously using a combination of protein-binding, mutational, and cross-linking approaches. In Escherichia coli, the switch from counterclockwise to clockwise rotation is triggered by the signaling protein phospho-CheY, which binds to the lower part of the switch complex and induces small movements of FliM and FliN subunits relative to each other. Direction switching also must produce movements in the upper part of the complex, particularly in the C-terminal domain of FliG (FliGC), which interacts with the stator to generate the torque for flagellar rotation. In the present study, protein movements in the middle and upper parts of the switch complex have been probed by means of targeted cross-linking and mutational analysis. Switching induces a tilting movement of the FliM domains that form the middle part of the switch and a consequent rotation of the affixed FliGC domains that reorients the stator interaction sites by about 90°. In a recently proposed hypothesis for the motor mechanism, such a reorientation of FliGC would reverse the direction of motor rotation