Controlling the uncontrollable: Quantum control of open-system dynamics.

Control of open quantum systems is essential for the realization of contemporary quantum science and technology. We demonstrate such control using a thermodynamically consistent framework, taking into account the fact that the drive can modify the system's interaction with the environment. Such an effect is incorporated within the dynamical equation, leading to control-dependent dissipation.

Variational Solutions for Resonances by a Finite-Difference Grid Method.

We demonstrate that the finite difference grid method (FDM) can be simply modified to satisfy the variational principle and enable calculations of both real and complex poles of the scattering matrix. These complex poles are known as resonances and provide the energies and inverse lifetimes of the system under study (e.g.

Quantum Finite-Time Thermodynamics: Insight from a Single Qubit Engine.

Incorporating time into thermodynamics allows for addressing the tradeoff between efficiency and power. A qubit engine serves as a toy model in order to study this tradeoff from first principles, based on the quantum theory of open systems. We study the quantum origin of irreversibility, originating from heat transport, quantum friction, and thermalization in the presence of external driving.

Shortcut to Equilibration of an Open Quantum System.

We present a procedure to accelerate the relaxation of an open quantum system towards its equilibrium state. The control protocol, termed the shortcut to equilibration, is obtained by reverse-engineering the nonadiabatic master equation. This is a nonunitary control task aimed at rapidly changing the entropy of the system.

Preliminary crystallographic analysis of Xyn52B2, a GH52 β-D-xylosidase from Geobacillus stearothermophilus T6.

Geobacillus stearothermophilus T6 is a thermophilic bacterium that possesses an extensive hemicellulolytic system, including over 40 specific genes that are dedicated to this purpose. For the utilization of xylan, the bacterium uses an extracellular xylanase which degrades xylan to decorated xylo-oligomers that are imported into the cell. These oligomers are hydrolyzed by side-chain-cleaving enzymes such as arabinofuranosidases, acetylesterases and a glucuronidase, and finally by an intracellular xylanase and a number of β-xylosidases.

Cloning, purification and preliminary crystallographic analysis of Ara127N, a GH127 β-L-arabinofuranosidase from Geobacillus stearothermophilus T6.

The L-arabinan utilization system of Geobacillus stearothermophilus T6 is composed of five transcriptional units that are clustered within a 38 kb DNA segment. One of the transcriptional units contains 11 genes, the last gene of which (araN) encodes a protein, Ara127N, that belongs to the newly established GH127 family. Ara127N shares 44% sequence identity with the recently characterized HypBA1 protein from Bifidobacterium longum and thus is likely to function similarly as a β-L-arabinofuranosidase.

Purification, crystallization and preliminary crystallographic analysis of Gan1D, a GH1 6-phospho-β-galactosidase from Geobacillus stearothermophilus T1.

Geobacillus stearothermophilus T1 is a Gram-positive thermophilic soil bacterium that contains an extensive system for the utilization of plant cell-wall polysaccharides, including xylan, arabinan and galactan. The bacterium uses a number of extracellular enzymes that break down the high-molecular-weight polysaccharides into short oligosaccharides, which enter the cell and are further hydrolyzed into sugar monomers by dedicated intracellular glycoside hydrolases. The interest in the biochemical characterization and structural analysis of these proteins originates mainly from the wide range of their potential biotechnological applications.