We cloned the genes encoding the ribosomal proteins Ph (Pyrococcus horikoshii)-P0, Ph-L12 and Ph-L11, which constitute the GTPase-associated centre of the archaebacterium Pyrococcus horikoshii. These proteins are homologues of the eukaryotic P0, P1/P2 and eL12 proteins, and correspond to Escherichia coli L10, L7/L12 and L11 proteins respectively. The proteins and the truncation mutants of Ph-P0...

The onset of chemical order L10 phase and perpendicular magnetic anisotropy in FePd 001 thin films sputtered on MgO 001 at temperatures from room temperature to 700 °C and thickness between 1.4 and 22 nm are investigated. It is found that the formation of the FePd ordered phase exhibiting high perpendicular magnetic anisotropy L10 phase with the c axis in the growth direction is affected by a t...

We present a study of the magnetic properties of arrays of nanostructures produced in a focussed ion beam–scanning electron microscope dual beam system. The single magnetic units have been isolated either by direct removal of parts of the metallic film or by local modification of the film magnetic properties. The final quality of the shape and the residual damage strictly depend on beam paramet...

Utilizing first-principles atomistic simulations we present a twin nucleation model based on the Peierls–Nabarro formulation. We investigated twinning in several important shape memory alloys, starting with Ni2FeGa (14M modulated monoclinic and L10 crystals) to illustrate the methodology, and predicted the twin stress in Ni2MnGa, NiTi, Co2NiGa, and Co2NiAl martensites, all of which were in exce...

In this work, we studied the effects of Sn addition on the ordering temperature of FePt thin film. The coercivity of FePtSn film was about 1000 Oe greater than the coercivity of FePt film for an annealing temperature of 600C. Therefore, Sn addition was effective in promoting the L10 ordering and in reducing the ordering temperature of the FePt film. From our X-ray diffraction results, we found ...

The ribosomal stalk in bacteria is composed of four or six copies of L12 proteins arranged in dimers that bind to the adjacent sites on protein L10, spanning 10 amino acids each from the L10 C-terminus. To study why multiple L12 dimers are required on the ribosome, we created a chromosomally engineered Escherichia coli strain, JE105, in which the peripheral L12 dimer binding site was deleted. T...

ANDREA BENEDETTI, PhD†‡¶, MARK S. GOLDBERG, PhD†‡§, and MICHAL ABRAHAMOWICZ, PhD†║ † McGill University, Department of Epidemiology, Biostatistics and Occupational Health, Montreal, Canada ‡ McGill University, Department of Medicine, Montreal, Canada ¶ Montreal Chest Institute, Respiratory Epidemiology and Clinical Research Unit, Montreal, Canada §Royal Victoria Hospital, Division of Clinical Ep...