Low-Complexity Calibration of Mutually Coupled Non-Reciprocal Multi-Antenna OFDM Transceivers

Abstract—In adaptive time division duplex (TDD) broadcast multi-antenna orthogonal frequency division multiplexing (OFDM) systems, non-reciprocal transceiver chains at the base station (BS) cause multi-user interference. This is due to the inappropriate spatial filter design at the BS based on the reverse link estimate. Hence, BS transceiver calibration is required. Provided that an estimate of the forward link channel is available at the BS, e.g., in a calibration phase, the transceiver parameters can be estimated by solving a total least squares (TLS) problem. In addition, if mutual coupling between the antennas exists the number of unknown front-end parameters to be estimated increases. Consequently, large matrices need to be decomposed via singular value decomposition (SVD) to attain a calibrated system. To deal with these large matrices a conjugate gradient (CG) method for solving the TLS problem iteratively is proposed in this paper. Simulation results show that the calibration based on the CG method achieves almost the same performance compared to the TLS solution but with significantly reduced complexity. I

The Protein Targeting Factor Get3 Functions as ATP-Independent Chaperone under Oxidative Stress Conditions

Exposure of cells to reactive oxygen species (ROS) causes a rapid and significant drop in intracellular ATP levels. This energy depletion negatively affects ATP-dependent chaperone systems, making ROS-mediated protein unfolding and aggregation a potentially very challenging problem. Here we show that Get3, a protein involved in ATP-dependent targeting of tail-anchored (TA) proteins under nonstress conditions, turns into an effective ATP-independent chaperone when oxidized. Activation of Get3's chaperone function, which is a fully reversible process, involves disulfide bond formation, metal release, and its conversion into distinct, higher oligomeric structures. Mutational studies demonstrate that the chaperone activity of Get3 is functionally distinct from and likely mutually exclusive with its targeting function, and responsible for the oxidative stress-sensitive phenotype that has long been noted for yeast cells lacking functional Get3. These results provide convincing evidence that Get3 functions as a redox-regulated chaperone, effectively protecting eukaryotic cells against oxidative protein damage