Search for: All records

AST3-2 is the second of the three Antarctic Survey Telescopes, aimed at wide-field time-domain optical astronomy. It is located at Dome A, Antarctica, which is by many measures the best optical astronomy site on the Earth’s surface. Here we present the data from the AST3-2 automatic survey in 2016 and the photometry results. The median 5σ limiting magnitude in i-band is 17.8 mag and the light-curve precision is 4 mmag for bright stars. The data release includes photometry for over 7 million stars, from which over 3500 variable stars were detected, with 70 of them newly discovered. We classify these new variables into different types by combining their light-curve features with stellar properties from surveys such as StarHorse.

 

While amber suppression is the most common approach to introduce noncanonical amino acids into proteins in live cells, quadruplet codon decoding has potential to enable a greatly expanded genetic code with up to 256 new codons for protein biosynthesis. Since triplet codons are the predominant form of genetic code in nature, quadruplet codon decoding often displays limited efficiency. In this work, we exploited a new approach to significantly improve quadruplet UAGN and AGGN (N = A, U, G, C) codon decoding efficiency by using recoding signals imbedded in mRNA. With representative recoding signals, the expression level of mutant proteins containing UAGN and AGGN codons reached 48% and 98% of that of the wild-type protein, respectively. Furthermore, this strategy mitigates a common concern of reading-through endogenous stop codons with amber suppression-based system. Since synthetic recoding signals are rarely found near the endogenous UAGN and AGGN sequences, a low level of undesirable suppression is expected. Our strategy will greatly enhance the utility of noncanonical amino acid mutagenesis in live-cell studies.

 

Protein tyrosineO-sulfation (PTS) plays a crucial role in extracellular biomolecular interactions that dictate various cellular processes. It also involves in the development of many human diseases. Regardless of recent progress, our current understanding of PTS is still in its infancy. To promote and facilitate relevant studies, a generally applicable method is needed to enable efficient expression of sulfoproteins with defined sulfation sites in live mammalian cells. Here we report the engineering, in vitro biochemical characterization, structural study, and in vivo functional verification of a tyrosyl-tRNA synthetase mutant for the genetic encoding of sulfotyrosine in mammalian cells. We further apply this chemical biology tool to cell-based studies on the role of a sulfation site in the activation of chemokine receptor CXCR4 by its ligand. Our work will not only facilitate cellular studies of PTS, but also paves the way for economical production of sulfated proteins as therapeutic agents in mammalian systems.

 

The microstructure of FeCuB ribbons (∼20 μm thick) was modified to fabricate α′′-Fe 16 N 2 at a temperature as low as 160 °C. The ribbon samples were heat treated first at a temperature reaching 930 °C and then quenched down to room temperature. During the heat treatment, ribbon samples were oxidized, and hydrogen reduction was then conducted to remove the oxygen from the ribbon samples. The reduced ribbon samples had a porous structure, which improved the nitrogen diffusion efficiency and decreased the fabrication temperature of α′′-Fe 16 N 2 down to 160 °C. It was demonstrated that the techniques for microstructure control in this method including oxidation and reduction helped obtain the α′′-Fe 16 N 2 phase with high coercivity, thus manifesting this could be a promising technique for low-temperature nitridation on ribbons in general. 

Understanding the nucleon spin structure in the regime where the strong interaction becomes truly strong poses a challenge to both experiment and theory. At energy scales below the nucleon mass of about 1 GeV, the intense interaction among the quarks and gluons inside the nucleon makes them highly correlated. Their coherent behaviour causes the emergence of effective degrees of freedom, requiring the application of non-perturbative techniques such as chiral effective field theory. Here we present measurements of the neutron’s generalized spin polarizabilities that quantify the neutron’s spin precession under electromagnetic fields at very low energy-momentum transfer squared down to 0.035 GeV2. In this regime, chiral effective field theory calculations are expected to be applicable. Our data, however, show a strong discrepancy with these predictions, presenting a challenge to the current description of the neutron’s spin properties.