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   https://doi.org/10.1021/acs.analchem.0c00829  

   Dong, Shiyu; Shirzadeh, Mehdi; Fan, Liqi; Laganowsky, Arthur; Russell, David H. (July 2020, Analytical Chemistry)

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   https://doi.org/10.1021/acs.biochem.8b00300  

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3. The Neumann problem on the domain in 𝕊 ³ bounded by the Clifford torus

   https://doi.org/10.1515/ans-2022-0072  

   Case, Jeffrey S; Chen, Eric; Wang, Yi; Yang, Paul; Yung, Po-Lam (January 2023, Advanced Nonlinear Studies)

   Abstract In this study, the solution of the Neumann problem associated with the CR Yamabe operator on a subset $\mathrm{\Omega }$\Omegaof the CR manifold ${\mathbb{S}}^3${{\mathbb{S}}}^{3}bounded by the Clifford torus $\mathrm{\Sigma }$\Sigmais discussed. The Yamabe-type problem of finding a contact form on $\mathrm{\Omega }$\Omegawhich has zero Tanaka-Webster scalar curvature and for which $\mathrm{\Sigma }$\Sigmahas a constant $p$p-mean curvature is also discussed. 

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4. Mapping temperature-dependent conformational change in the voltage-sensing domain of an engineered heat-activated K ⁺ channel

   https://doi.org/10.1073/pnas.2017280118  

   Chen, Hongbo; Deng, Jiahua; Cui, Qiang; Chanda, Baron; Henzler-Wildman, Katherine (March 2021, Proceedings of the National Academy of Sciences)

   Temperature-dependent regulation of ion channel activity is critical for a variety of physiological processes ranging from immune response to perception of noxious stimuli. Our understanding of the structural mechanisms that underlie temperature sensing remains limited, in part due to the difficulty of combining high-resolution structural analysis with temperature stimulus. Here, we use NMR to compare the temperature-dependent behavior of Shaker potassium channel voltage sensor domain (WT-VSD) to its engineered temperature sensitive (TS-VSD) variant. Further insight into the molecular basis for temperature-dependent behavior is obtained by analyzing the experimental results together with molecular dynamics simulations. Our studies reveal that the overall secondary structure of the engineered TS-VSD is identical to the wild-type channels except for local changes in backbone torsion angles near the site of substitution (V369S and F370S). Remarkably however, these structural differences result in increased hydration of the voltage-sensing arginines and the S4–S5 linker helix in the TS-VSD at higher temperatures, in contrast to the WT-VSD. These findings highlight how subtle differences in the primary structure can result in large-scale changes in solvation and thereby confer increased temperature-dependent activity beyond that predicted by linear summation of solvation energies of individual substituents. 

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5. ¹⁹ F Fast Magic-Angle Spinning NMR Spectroscopy on Microcrystalline Complexes of Fluorinated Ligands and the Carbohydrate Recognition Domain of Galectin-3

   https://doi.org/10.1021/acs.biochem.4c00232  

   Kalabekova, Roza; Quinn, Caitlin M; Movellan, Kumar Tekwani; Gronenborn, Angela M; Akke, Mikael; Polenova, Tatyana (September 2024, Biochemistry)