The Temptation and Fall of Original Understanding

Review of: The Tempting of America: The Political Seduction of the Law, by Robert H. Bork (Free Press, 1990

A demonstration of motion base design alternatives for the National Advanced Driving Simulator

A demonstration of the capability of NASA's Vertical Motion Simulator to simulate two alternative motion base designs for the National Advanced Driving simulator (NADS) is reported. The VMS is located at ARC. The motion base conditions used in this demonstration were as follows: (1) a large translational motion base; and (2) a motion base design with limited translational capability. The latter had translational capability representative of a typical synergistic motion platform. These alternatives were selected to test the prediction that large amplitude translational motion would result in a lower incidence or severity of simulator induced sickness (SIS) than would a limited translational motion base. A total of 10 drivers performed two tasks, slaloms and quick-stops, using each of the motion bases. Physiological, objective, and subjective measures were collected. No reliable differences in SIS between the motion base conditions was found in this demonstration. However, in light of the cost considerations and engineering challenges associated with implementing a large translation motion base, performance of a formal study is recommended

Acid-Base Chemical Mechanism of Aspartase From Hafnia alvei

An acid-base chemical mechanism is proposed for Hafnia alvei aspartase in which a proton is abstracted from C-3 of the monoanionic form of L-aspartate by an enzyme general base with a pK of 6.3-6.6 in the absence and presence of Mg2+. The resulting carbanion is presumably stabilized by delocalization of electrons into the β-carboxyl with the assistance of a protonated enzyme group in the vicinity of the β-carboxyl. Ammonia is then expelled with the assistance of a general acid group that traps an initially expelled NH3 as the final NH+4 product. In agreement with the function of the general acid group, potassium, an analog of NH+4, binds optimally when the group is unprotonated. The pK for the general acid is about 7 in the absence of Mg2+, but is increased by about a pH unit in the presence of Mg2+. Since the same pK values are observed in the pKisuccinate and V/K pH profile, both enzyme groups must be in their optimum protonation state for efficient binding of reactant in the presence of Mg2+. At the end of a catalytic cycle, both the general base and general acid groups are in a protonation state opposite that in which they started when aspartate was bound. The presence of Mg2+ causes a pH-dependent activation of aspartase exhibited as a partial change in the V and V/Kasp pH profiles. When the aspartase reaction is run in D2O to greater than 50% completion no deuterium is found in the remaining aspartate, indicating that the site is inaccessible to solvent during the catalytic cycle

Launching a Journal About and Through Students as Partners

Editorial of first issue of the International Journal for Student as Partners