https://www.selleckchem.com/products/navoximod.html Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for analyzing protein structure, interaction, and dynamics at atomic resolution and in various sample states including solution state, solid state, and membranous environment. Thanks to rapid NMR methodology development, the past decade has witnessed a growing number of protein NMR studies in complex systems ranging from membrane mimetics to living cells, which pushes the research frontier further toward physiological environments and offers unique insights in elucidating protein functional mechanisms. In particular, in-cell NMR has become a method of choice for bridging the huge gap between structural biology and cell biology. Herein, we review the recent developments and applications of NMR methods for protein analysis in close-to-physiological environments, with special emphasis on in-cell protein structural determination and the analysis of protein dynamics, both difficult to be accessed by traditional methods.Si is a well-known high-capacity lithium-ion battery anode material; however, it suffers from conductivity and volume expansion issues. Herein, we develop a "surface oxidation" strategy to introduce a SiOx layer on Si nanoparticles for subsequent carbon coating. It is found that the surface SiOx layer could facilitate the conformal resin coating process through strong interactions with phenolic resin, and well-defined core@double-shell-structured Si@SiOx@C can be obtained after further carbonization. Without the surface SiOx layer, only a negligible fraction of Si nanoparticles can be encapsulated into the carbon matrix. With enhanced conductivity and confined volume change, Si@SiOx@C demonstrates high reversible capacity as well as long-term durability.In virtue of the inherent molecular recognition and programmability, DNA has recently become the most promising for high-performance biosensors. The rationally engineered nucleic ac