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1. Laser-cooling Cadmium Bosons and Fermions with Near Ultraviolet Triplet Excitations

   https://doi.org/10.1088/1742-6596/2889/1/012006  

   Gibble, Kurt (November 2024, Journal of Physics: Conference Series)

   Abstract Cadmium is laser-cooled and trapped with excitations to triplet states with UVA light, first using only the 67 kHz wide 326 nm intercombination line and subsequently, for large loading rates, the 25 MHz wide 361 nm³P₂→³D₃transition. Eschewing the hard UV 229 nm¹S₀→¹P₁transition, only small magnetic fields gradients, less than 6 G cm⁻¹, are required enabling a 100% transfer of atoms from the 361 nm trap to the 326 nm narrow-line trap. All 8 stable cadmium isotopes are straightforwardly trapped, including two nuclear-spin- $\frac{1}{2}$fermions that require no additional repumping. We observe evidence of³P₂collisions limiting the number of trapped metastable atoms, report isotope shifts for¹¹¹Cd and¹¹³Cd of the 326 nm¹S₀→³P₁, 480nm³P₁→³S₁, and 361 nm³P₂→³D₃transitions, and measure the¹¹⁴Cd 5s5p³P₂→ 5s5d³D₃transition frequency to be 830 096 573(15) MHz. 

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2. Long-range dynamic correlations regulate the catalytic activity of the bacterial tyrosine kinase Wzc

   https://doi.org/10.1126/sciadv.abd3718  

   Hajredini, Fatlum; Piserchio, Andrea; Ghose, Ranajeet (December 2020, Science Advances)

   null (Ed.)

   BY-kinases represent a highly conserved family of protein tyrosine kinases unique to bacteria without eukaryotic orthologs. BY-kinases are regulated by oligomerization-enabled transphosphorylation on a C-terminal tyrosine cluster through a process with sparse mechanistic detail. Using the catalytic domain (CD) of the archetypal BY-kinase, Escherichia coli Wzc, and enhanced-sampling molecular dynamics simulations, isothermal titration calorimetry and nuclear magnetic resonance measurements, we propose a mechanism for its activation and nucleotide exchange. We find that the monomeric Wzc CD preferentially populates states characterized by distortions at its oligomerization interfaces and by catalytic element conformations that allow high-affinity interactions with ADP but not with ATP·Mg 2+ . We propose that oligomer formation stabilizes the intermonomer interfaces and results in catalytic element conformations suitable for optimally engaging ATP·Mg 2+ , facilitating exchange with bound ADP. This sequence of events, oligomerization, i.e., substrate binding, before engaging ATP·Mg 2+ , facilitates optimal autophosphorylation by preventing a futile cycle of ATP hydrolysis. 

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3. Gelsolin-mediated actin filament severing, mechanics, and conformational changes at neutral and acidic pH

   https://doi.org/10.3389/frsfm.2025.1530439  

   Douglas, Taylor V; Toland, Claire A; Paulin, Sydney A; Castaneda, Nicholas; Tetard, Laurene; Kang, Ellen H (March 2025, Frontiers in Soft Matter)

   Gelsolin is a calcium (Ca²⁺) dependent, pH sensitive actin-binding protein that regulates actin filament dynamics to remodel the actin cytoskeleton. It is known that gelsolin binding induces conformational changes of actin filaments, leading to filament severing. However, the influence of physiological conditions, such as pH variations, on gelsolin-mediated filament severing activities, mechanics and conformations remains unclear despite their role in actin-actin interactions. Using Total Internal Reflection Fluorescence (TIRF) microscopy imaging and pyrene fluorescence assays, we demonstrate that filament severing efficiencies by gelsolin are enhanced in acidic conditions. In addition, analysis of filament thermal fluctuations using TIRF reveals that gelsolin binding stiffens actin filaments. Furthermore, we show that gelsolin binding induces conformational changes in filaments by measuring the filament half-pitch using high resolution Atomic Force Microscopy imaging. Together, our results suggest that pH modulation plays a key role in gelsolin-mediated filament severing activities, bending mechanics, and conformational changes, which have implications in many cellular processes including cell motility and morphogenesis. 

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4. Brown Dwarf Retrievals on FIRE!: Atmospheric Constraints and Lessons Learned from High Signal-to-noise Medium-resolution Spectroscopy of a T9 Dwarf

   https://doi.org/10.3847/1538-4357/ace32e  

   Hood, Callie E; Fortney, Jonathan J; Line, Michael R; Faherty, Jacqueline K (August 2023, The Astrophysical Journal)

   Abstract Brown dwarf spectra offer vital testbeds for our understanding of the chemical and physical processes that sculpt substellar atmospheres. Recently, atmospheric retrieval approaches have been successfully applied to low-resolution (R∼ 100) spectra of L, T, and Y dwarfs, yielding constraints on the chemical abundances and temperature structures of these atmospheres. Medium-resolution (R∼ 10³) spectra of brown dwarfs offer additional insight, as molecular features are more easily disentangled and the thermal structure of the upper atmosphere is better probed. We present results from a GPU-based retrieval analysis of a high signal-to-noise, medium-resolution (R∼ 6000) FIRE spectrum from 0.85 to 2.5μm of the T9 dwarf UGPS J072227.51–054031.2. At 60× higher spectral resolution than previous brown dwarf retrievals, a number of novel challenges arise. We examine the effect of different opacity sources, in particular for CH₄. Furthermore, we find that flaws in the data like errors from order stitching can bias our constraints. We compare these retrieval results to those for anR∼ 100 spectrum of the same object, revealing how constraints on atmospheric abundances and temperatures improve by an order of magnitude or more with increased spectral resolution. In particular, we can constrain the abundance of H₂S, which is undetectable at lower spectral resolution. While these medium-resolution retrievals offer the potential of precise, stellar-like constraints on atmospheric abundances (∼0.02 dex), our retrieved radius is unphysically small ( $R={0.50}_{-0.01}^{+0.01}$R_Jup), indicating shortcomings with our modeling framework. This work is an initial investigation into brown dwarf retrievals at medium spectral resolution, offering guidance for future ground-based studies and JWST observations. 

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5. Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo

   https://doi.org/10.1038/s41467-023-42037-4  

   Mendoza, Johnny; Purchal, Meredith; Yamada, Kazuhiro; Koutmos, Markos (December 2023, Nature Communications)

   Abstract Cobalamin-dependent methionine synthase (MS) is a key enzyme in methionine and folate one-carbon metabolism. MS is a large multi-domain protein capable of binding and activating three substrates: homocysteine, folate, andS-adenosylmethionine for methylation. Achieving three chemically distinct methylations necessitates significant domain rearrangements to facilitate substrate access to the cobalamin cofactor at the right time. The distinct conformations required for each reaction have eluded structural characterization as its inherently dynamic nature renders structural studies difficult. Here, we use a thermophilic MS homolog (tMS) as a functional MS model. Its exceptional stability enabled characterization of MS in the absence of cobalamin, marking the only studies of a cobalamin-binding protein in its apoenzyme state. More importantly, we report the high-resolution full-length MS structure, ending a multi-decade quest. We also capture cobalamin loadingin crystallo, providing structural insights into holoenzyme formation. Our work paves the way for unraveling how MS orchestrates large-scale domain rearrangements crucial for achieving challenging chemistries. 

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