2 research outputs found
Demonstration of a parity-time symmetry breaking phase transition using superconducting and trapped-ion qutrits
Scalable quantum computers hold the promise to solve hard computational
problems, such as prime factorization, combinatorial optimization, simulation
of many-body physics, and quantum chemistry. While being key to understanding
many real-world phenomena, simulation of non-conservative quantum dynamics
presents a challenge for unitary quantum computation. In this work, we focus on
simulating non-unitary parity-time symmetric systems, which exhibit a
distinctive symmetry-breaking phase transition as well as other unique features
that have no counterpart in closed systems. We show that a qutrit, a
three-level quantum system, is capable of realizing this non-equilibrium phase
transition. By using two physical platforms - an array of trapped ions and a
superconducting transmon - and by controlling their three energy levels in a
digital manner, we experimentally simulate the parity-time symmetry-breaking
phase transition. Our results indicate the potential advantage of multi-level
(qudit) processors in simulating physical effects, where additional accessible
levels can play the role of a controlled environment.Comment: 14 pages, 9 figure
Effect of Arginine on Chaperone-Like Activity of HspB6 and Monomeric 14-3-3ζ
The effect of protein chaperones HspB6 and the monomeric form of the protein 14-3-3ζ (14-3-3ζm) on a test system based on thermal aggregation of UV-irradiated glycogen phosphorylase b (UV-Phb) at 37 °C and a constant ionic strength (0.15 M) was studied using dynamic light scattering. A significant increase in the anti-aggregation activity of HspB6 and 14-3-3ζm was demonstrated in the presence of 0.1 M arginine (Arg). To compare the effects of these chaperones on UV-Phb aggregation, the values of initial stoichiometry of the chaperone–target protein complex (S0) were used. The analysis of the S0 values shows that in the presence of Arg fewer chaperone subunits are needed to completely prevent aggregation of the UV-Phb subunit. The changes in the structures of HspB6 and 14-3-3ζm induced by binding of Arg were evaluated by the fluorescence spectroscopy and differential scanning calorimetry. It was suggested that Arg caused conformational changes in chaperone molecules, which led to a decrease in the thermal stability of protein chaperones and their destabilization