Nowa wersja platformy, zawierająca wyłącznie zasoby pełnotekstowe, jest już dostępna.
Przejdź na https://bibliotekanauki.pl
Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 19

Liczba wyników na stronie
first rewind previous Strona / 1 next fast forward last
Wyniki wyszukiwania
help Sortuj według:

help Ogranicz wyniki do:
first rewind previous Strona / 1 next fast forward last
XX
The gene for thermostable farnesyl diphosphate synthase from Bacillus stearothermophilus was cloned, sequenced, and overexpressed in Escherichia coli. The synthase was purified to homogeneity and crystallized. The enzyme carried only two cysteine residues in contrast to its counterparts from other sources, which have four to six cysteine residues. Either or both of the cysteine residues can be replaced with serine without causing a loss of the catalytic activity. The conserved arginine residue that occupies the third position from the C-terminus was also replaced with valine without significant loss of activity, but the valine mutant showed a weakened affinity for isopentenyl diphosphate.
EN
A few micrometers-sized Fe1-xAlx (x=0.35-0.42) powders prepared by atomizing method have the B2 structure and are paramegnetic. The powder milled for several hours is magnetized and has a spontaneous magnetization as great as 100 emu/g. The milled powder particles become flakes, which are composed of lamellae expanding parallel to the (110) plane and having heavily distorted lattice. High-resolution transmission electron microscopy and electron diffraction revealed that structures appear in very thin areas within the lamellae. These superlattices indicate the creation of large number of antiphase boundaries, which induce ferromagnetism. When the milled powder is heated at 100-400 degrees centigrade the magnetization decreases to a few tens emu/g, the lamella structures being kept.
first rewind previous Strona / 1 next fast forward last
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.