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Your search keyword '"Ding, H. -T."' showing total 2 results
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2 results on '"Ding, H. -T."'

1. In-medium bottomonium properties from lattice NRQCD calculations with extended meson operators

Author

Ding, H. -T., Huang, W. -P., Larsen, R., Meinel, S., Mukherjee, Swagato, Petreczky, P., and Tang, Zhanduo

Subjects
High Energy Physics - Lattice, High Energy Physics - Phenomenology, Nuclear Theory
Abstract

We calculate the temperature dependence of bottomonium correlators in (2+1)-flavor lattice QCD with the aim to constrain in-medium properties of bottomonia at high temperature. The lattice calculations are performed using HISQ action with physical strange quark mass and light quark masses twenty times smaller than the strange quark mass at two lattice spacings $a=0.0493$ fm and $0.0602$ fm, and temporal extents $N_{\tau}=16-30$, corresponding to the temperatures $T=133-250$ MeV. We use a tadpole-improved NRQCD action including spin-dependent $v^6$ corrections for the heavy quarks and extended meson operators in order to be sensitive to in-medium properties of the bottomonium states of interest. We find that within estimated errors the bottomonium masses do not change compared to their vacuum values for all temperatures under our consideration; however, we find different nonzero widths for the various bottomonium states., Comment: 13 pages main text + 7 pages appendix

Published
2025

2. Structural basis of a microbial trimethylamine transporter.

Author

Gao C, Ding H-T, Li K, Cao H-Y, Wang N, Gu Z-T, Wang Q, Sun M-L, Chen X-L, Chen Y, Zhang Y-Z, Fu H-H, and Li C-Y

Subjects
Membrane Transport Proteins metabolism, Membrane Transport Proteins chemistry, Membrane Transport Proteins genetics, Cryoelectron Microscopy, Protein Conformation, Models, Molecular, Biological Transport, Bacterial Proteins metabolism, Bacterial Proteins chemistry, Bacterial Proteins genetics, Protein Binding, Methylamines metabolism
Abstract

Trimethylamine (TMA), a simple trace biogenic amine resulting from the decomposition of proteins and other macromolecules, is ubiquitous in nature. It is found in the human gut as well as in various terrestrial and marine ecosystems. While the role of TMA in promoting cardiovascular diseases and depolarizing olfactory sensory neurons in humans has only recently been explored, many microbes are well known for their ability to utilize TMA as a carbon, nitrogen, and energy source. Here, we report the first structure of a TMA transporter, TmaT, originally identified from a marine bacterium. TmaT is a member of the betaine-choline-carnitine transporter family, and we show that TmaT is an Na + /TMA symporter, which possessed high specificity and binding affinity toward TMA. Furthermore, the structures of TmaT and two TmaT-TMA complexes were solved by cryo-EM. TmaT forms a homotrimer structure in solution. Each TmaT monomer has 12 transmembrane helices, and the TMA transport channel is formed by a four-helix bundle. TMA can move between different aromatic boxes, which provides the structural basis of TmaT importing TMA. When TMA is bound in location I, residues Trp146, Trp151, Tyr154, and Trp326 form an aromatic box to accommodate TMA. Moreover, Met105 also plays an important role in the binding of TMA. When TMA is transferred to location II, it is bound in the aromatic box formed by Trp325, Trp326, and Trp329. Based on our results, we proposed the TMA transport mechanism by TmaT. This study provides novel insights into TMA transport across biological membranes., Importance: The volatile trimethylamine (TMA) plays an important role in promoting cardiovascular diseases and depolarizing olfactory sensory neurons in humans and serves as a key nutrient source for a variety of ubiquitous marine microbes. While the TMA transporter TmaT has been identified from a marine bacterium, the structure of TmaT and the molecular mechanism involved in TMA transport remain unclear. In this study, we elucidated the high-resolution cryo-EM structures of TmaT and TmaT-TMA complexes and revealed the TMA binding and transport mechanisms by structural and biochemical analyses. The results advance our understanding of the TMA transport processes across biological membranes., Competing Interests: The authors declare no conflict of interest.

Published
2025
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