RESUMEN
We propose and analyze a novel mechanism for long-range spin-spin interactions in diamond nanostructures. The interactions between electronic spins, associated with nitrogen-vacancy centers in diamond, are mediated by their coupling via strain to the vibrational mode of a diamond mechanical nanoresonator. This coupling results in phonon-mediated effective spin-spin interactions that can be used to generate squeezed states of a spin ensemble. We show that spin dephasing and relaxation can be largely suppressed, allowing for substantial spin squeezing under realistic experimental conditions. Our approach has implications for spin-ensemble magnetometry, as well as phonon-mediated quantum information processing with spin qubits.
RESUMEN
We describe a method to create effective gauge potentials for stationary-light polaritons. When stationary light is created in the interaction with a rotating ensemble of coherently driven double-Lambda type atoms, the equation of motion is that of a massive Schrödinger particle in a magnetic field. Since the effective interaction area for the polaritons can be made large, degenerate Landau levels can be created with degeneracy well above 100. This opens up the possibility to study the bosonic analogue of the fractional quantum Hall effect for interacting stationary-light polaritons.
RESUMEN
We consider the interaction of two weak probe fields of light with an atomic ensemble coherently driven by two pairs of standing wave laser fields in a tripod-type linkage scheme. The system is shown to exhibit a Dirac-like spectrum for light-matter quasiparticles with multiple dark states, termed spinor slow-light polaritons. They posses an "effective speed of light" given by the group velocity of slow light, and can be made massive by inducing a small two-photon detuning. Control of the two-photon detuning can be used to locally vary the mass including a sign flip. Particularly, this allows the implementation of the random-mass Dirac model for which localized zero-energy (midgap) states exist with unusual long-range correlations.
RESUMEN
We discuss the properties of 1D stationary pulses of light in an atomic ensemble with electromagnetically induced transparency in the limit of tight spatial confinement. When the size of the wave packet becomes comparable or smaller than the absorption length of the medium, it must be described by a two-component vector which obeys the one-dimensional two-component Dirac equation with an effective mass m;{*} and effective speed of light c;{*}. Then a fundamental lower limit to the spatial width in an external potential arises from Klein tunneling and is given by the effective Compton length lambda_{C}=variant Planck's over 2pi/(m;{*}c;{*}). Since c;{*} and m;{*} can be externally controlled and can be made small, it is possible to observe effects of the relativistic dispersion for rather low energies or correspondingly on macroscopic length scales.
RESUMEN
Transglutaminases (TGases, EC 2.3.2.13) have proved to be valuable enzymes for site-directed protein coupling via N(epsilon)-(gamma-L-glutamyl)lysine bonds. Their use in conjugate synthesis would overcome many problems caused by chemical reagents. In this approach, we show for the first time that two proteins with different functionalities, namely soybean peroxidase and protein G, can be cross-linked by bacterial TGase with retention of their activities. Soybean peroxidase and protein G were chosen for the enzymic preparation of a bifunctional conjugate among a series of other TGase substrates detected by enzymic incorporation of small fluorescent or biotinylated molecules. The highest yields of conjugate were obtained with a 15-fold excess of peroxidase in phosphate buffer, pH 7.0. Size exclusion chromatography enabled both purification of the conjugates and recovery of the starting materials. Analysis of bifunctionality revealed the coupling of protein G with an average of three peroxidase molecules.
Asunto(s)
Proteínas del Tejido Nervioso/metabolismo , Peroxidasa/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo , Transglutaminasas/metabolismo , Cadaverina/análogos & derivados , Cadaverina/química , Dipéptidos/química , Ensayo de Inmunoadsorción Enzimática , Colorantes Fluorescentes , Glutamina/química , Lisina/química , Proteínas del Tejido Nervioso/química , Proteínas del Tejido Nervioso/inmunología , Peroxidasa/química , Ingeniería de Proteínas/métodos , Proteínas Recombinantes/aislamiento & purificación , Glycine max/enzimología , Proteína Estafilocócica A/química , Proteína Estafilocócica A/metabolismo , Especificidad por Sustrato , Sulfonamidas/química , Transglutaminasas/químicaRESUMEN
The zymogen of bacterial transglutaminase was found during cultivation of Streptoverticillium mobaraense (DSMZ strain) using rabbit antibodies raised against the active enzyme. Ion-exchange chromatography at pH 5.0 yielded a highly purified pro-enzyme. Structure information was obtained by means of Edman degradation and analysis of PCR amplified nucleotide fragments. The data revealed an excess of negatively charged amino acids in the pro-region resulting in a decreased isoelectric point of the zymogen. Additionally, the new sequence gave rise to some modifications to the previously published hypothetical structure of prepro-transglutaminase derived from genomic DNA [Washizu, K., Ando, K., Koikeda, S., Hirose, S., Matsuura, A., Takagi, H., Motoki, M. & Takeuchi, K. (1994) Biosci. Biotechnol. Biochem. 58, 82-87]. Inactive transglutaminase, which carries an activation peptide of 45 amino acids, has a calculated molecular mass of 42445 Da. Its pro-region provides for both suppression of activity and increased thermostability. Furthermore, it could be shown that the micro-organism produces a protease which cleaves pro-transglutaminase at the C-side of Pro45. Rapid transformation of the mature enzyme also occurs by addition of other proteases. During conversion, 43 and 41 amino acid peptides are released by bovine trypsin and dispase from Bacillus polymyxa, respectively. The detection of endogenous substrates in the murein layer makes discussion of the physiological role of bacterial transglutaminases necessary.