Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Más filtros











Base de datos
Intervalo de año de publicación
1.
Nat Nanotechnol ; 19(5): 605-611, 2024 May.
Artículo en Inglés | MEDLINE | ID: mdl-38326467

RESUMEN

Single electron spins bound to multi-phosphorus nuclear spin registers in silicon have demonstrated fast (0.8 ns) two-qubit SWAP gates and long spin relaxation times (~30 s). In these spin registers, when the donors are ionized, the nuclear spins remain weakly coupled to their environment, allowing exceptionally long coherence times. When the electron is present, the hyperfine interaction allows coupling of the spin and charge degrees of freedom for fast qubit operation and control. Here we demonstrate the use of the hyperfine interaction to enact electric dipole spin resonance to realize high-fidelity ( F = 10 0 - 6 + 0 %) initialization of all the nuclear spins within a four-qubit nuclear spin register. By controllably initializing the nuclear spins to ⇓ ⇓ ⇓ , we achieve single-electron qubit gate fidelities of F = 99.78 ± 0.07% (Clifford gate fidelities of 99.58 ± 0.14%), above the fault-tolerant threshold for the surface code with a coherence time of T 2 * = 12 µ s .

2.
Biochem Mol Biol Int ; 40(2): 417-25, 1996 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-8896765

RESUMEN

Chitinase has been purified from the extract of cabbage stems with roots through successive steps of ammonium sulfate fractionation, Sephadex G-75 gel filtration, chromatofocusing and Sephacryl S-200 HR gel filtration. By these steps, the purity of the enzyme increased by 63 fold and the recovery of the enzyme activity was 18%. The purified enzyme was homogeneous when analyzed by SDS-PAGE. It showed an optimal pH of 6 and optimal temperature of 60 degrees C for hydrolysis of ethylene glycol chitin (EGC). The molecular mass of the enzyme was 41 kDa, as determined by SDS-PAGE. Heavy metal ions (1.5 mM) Ag+, Hg2+ and Fe2+, and chemical modification agents NAI (1 mM), NBS (0.5 mM) and CHD (0.5 mM) significantly or completely inhibited the activity of the enzyme. Substrate EGC at high concentrations also inhibited the activity. BSA (0.05%), Triton X-100 (0.5%) and glycerol (50%) provided significant protection of the enzyme from freezing inactivation.


Asunto(s)
Brassica/enzimología , Quitinasas/aislamiento & purificación , Quitinasas/metabolismo , Sulfato de Amonio , Cationes/farmacología , Quitina/análogos & derivados , Quitinasas/química , Cromatografía en Gel , Electroforesis en Gel de Poliacrilamida , Inhibidores Enzimáticos/farmacología , Estabilidad de Enzimas , Concentración de Iones de Hidrógeno , Cinética , Peso Molecular , Raíces de Plantas , Tallos de la Planta , Termodinámica
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA