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Creators/Authors contains: "Shao, Zhiwei"

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  1. ABSTRACT

    Using high-resolution Romulus simulations, we explore the origin and evolution of the circumgalactic medium (CGM) in the region 0.1 ≤ R/R500 ≤ 1 around massive central galaxies in group-scale halos. We find that the CGM is multiphase and highly dynamic. Investigating the dynamics, we identify seven patterns of evolution. We show that these are robust and detected consistently across various conditions. The gas cools via two pathways: (1) filamentary cooling inflows and (2) condensations forming from rapidly cooling density perturbations. In our cosmological simulations, the perturbations are mainly seeded by orbiting substructures. The condensations can form even when the median tcool/tff of the X-ray emitting gas is above 10 or 20. Strong amplitude perturbations can provoke runaway cooling regardless of the state of the background gas. We also find perturbations whose local tcool/tff ratios drop below the threshold but which do not condense. Rather, the ratios fall to some minimum value and then bounce. These are weak perturbations that are temporarily swept up in satellite wakes and carried to larger radii. Their tcool/tff ratios decrease because tff is increasing, not because tcool is decreasing. For structures forming hierarchically, our study highlights the challenge of using a simple threshold argument to infer the CGM’s evolution. It also highlights that the median hot gas properties are suboptimal determinants of the CGM’s state and dynamics. Realistic CGM models must incorporate the impact of mergers and orbiting satellites, along with the CGM’s heating and cooling cycles.

     
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  2. Abstract

    Cadmium (Cd) is one of the most toxic heavy metals. Exposure to Cd can impair the functions of the kidney, respiratory system, reproductive system and skeletal system. Cd2+-binding aptamers have been extensively utilized in the development of Cd2+-detecting devices; however, the underlying mechanisms remain elusive. This study reports four Cd2+-bound DNA aptamer structures, representing the only Cd2+-specific aptamer structures available to date. In all the structures, the Cd2+-binding loop (CBL-loop) adopts a compact, double-twisted conformation and the Cd2+ ion is mainly coordinated with the G9, C12 and G16 nucleotides. Moreover, T11 and A15 within the CBL-loop form one regular Watson–Crick pair and stabilize the conformation of G9. The conformation of G16 is stabilized by the G8–C18 pair of the stem. By folding and/or stabilizing the CBL-loop, the other four nucleotides of the CBL-loop also play important roles in Cd2+ binding. Similarly to the native sequence, crystal structures, circular dichroism spectrum and isothermal titration calorimetry analysis confirm that several variants of the aptamer can recognize Cd2+. This study not only reveals the underlying basis for the binding of Cd2+ ions with the aptamer, but also extends the sequence for the construction of novel metal–DNA complex.

     
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  3. Abstract

    Owing to its great threat to human health and environment, Pb2+pollution has been recognized as a major public problem by the World Health Organization (WHO). Many DNA aptamers have been utilized in the development of Pb2+-detection sensors, but the underlying mechanisms remain elusive. Here, we report three Pb2+-complexed structures of the thrombin binding aptamer (TBA). These high-resolution crystal structures showed that TBA forms intramolecular G-quadruplex and Pb2+is bound by the two G-tetrads in the center. Compared to K+-stabilized G-quadruplexes, the coordinating distance between Pb2+and the G-tetrads are much shorter. The T3T4 and T12T13 linkers play important roles in dimerization and crystallization of TBA, but they are changeable for Pb2+-binding. In combination with mutagenesis and CD spectra, the G8C mutant structure unraveled that the T7G8T9 linker of TBA is also variable. In addition to expansion of the Pb2+-binding aptamer sequences, our study also set up one great example for quick and rational development of other aptamers with similar or optimized binding activity.

     
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