Identifying Exchangeable Protons in a 1D NMR Spectrum by Spatially Selective Exchange-Editing.

The front cover artwork is provided by Markus Rotzinger at the University of Graz, Austria. The front cover picture illustrates the way the 1D exchange-editing NMR method makes exchanging protons visible by sign alteration. The depicted spectrum of D-glucose shows all exchanging signals inverted, thus allowing a fast qualitative determination, potentially in a single scan. Read the full text of the Research Article at 10.1002/cphc.202300713.

Identifying Exchangeable Protons in a 1D NMR Spectrum by Spatially Selective Exchange-Editing.

Signals undergoing chemical or conformational exchange in one-dimensional NMR spectra are often identified by deuterium exchange. In order to obtain quantitative information about the dynamic processes involved, one frequently used method is EXchange SpectroscopY (EXSY). To detect all exchange processes, the EXSY experiment requires the acquisition of time-consuming two-dimensional spectra. Here we report a faster alternative, an experiment which uses spatial encoding to extract similar information in a 1D exchange-edited experiment. Thereby, all protons are observed at once, but in different slices of the detection volume. The experiment can be carried out in a single scan to identify exchanging sites in a 1D spectrum by changes in signal intensity indicating exchange processes. If the exchanging partner, for example water is in molar excess the exchange-editing method easily identifies mobile protons by negative signals in the 1D 1H NMR spectrum.

Vibrio cholerae's ToxRS bile sensing system.

The seventh pandemic of the diarrheal cholera disease, which began in 1960, is caused by the Gram-negative bacterium Vibrio cholerae. Its environmental persistence provoking recurring sudden outbreaks is enabled by V. cholerae's rapid adaption to changing environments involving sensory proteins like ToxR and ToxS. Located at the inner membrane, ToxR and ToxS react to environmental stimuli like bile acid, thereby inducing survival strategies for example bile resistance and virulence regulation. The presented crystal structure of the sensory domains of ToxR and ToxS in combination with multiple bile acid interaction studies, reveals that a bile binding pocket of ToxS is only properly folded upon binding to ToxR. Our data proposes an interdependent functionality between ToxR transcriptional activity and ToxS sensory function. These findings support the previously suggested link between ToxRS and VtrAC-like co-component systems. Besides VtrAC, ToxRS is now the only experimentally determined structure within this recently defined superfamily, further emphasizing its significance. In-depth analysis of the ToxRS complex reveals its remarkable conservation across various Vibrio species, underlining the significance of conserved residues in the ToxS barrel and the more diverse ToxR sensory domain. Unravelling the intricate mechanisms governing ToxRS's environmental sensing capabilities, provides a promising tool for disruption of this vital interaction, ultimately inhibiting Vibrio's survival and virulence. Our findings hold far-reaching implications for all Vibrio strains that rely on the ToxRS system as a shared sensory cornerstone for adapting to their surroundings.

Cholera is a contagious diarrheal disease that leads to about 20,000 to 140,000 yearly deaths. It is caused by a bacterium called Vibrio cholerae, which can survive in harsh conditions and many environments. It often contaminates water, where it lives in an energy-conserving mode. But when humans consume Vibrio cholerae-contaminated water or food, the bacterium can sense its new environment and switch into a high-energy consuming state, causing fever, diarrhea, and vomiting. Vibrio cholerae recognizes bile acid in the human stomach, which signals that the bacterium has reached ideal conditions for causing disease. So far, it has been unclear, how exactly the bacterium detects bile acid. Understanding how these bacteria sense bile acid, could help scientists develop new ways to prevent cholera outbreaks or treat infections. Gubensäk et al. analysed two proteins from the Vibrio cholerae bacterium, called ToxR and ToxS, which are located below the bacteria's protective membrane. More detailed analyses showed that the two proteins bind together, forming a bile-binding pocket. When correctly assembled, this bile-sensing machine detects bile concentrations in the body, allowing the bacterium to adapt to the local conditions. Using crystal structures, a series of interaction studies, and modeling software, Gubensäk et al. detailed step-by-step how the two proteins sense bile acid and help the bacteria adapt and thrive in the human body. The results confirm the results of previous studies that implicated ToxR and ToxS in bile sensing and provide new details about the process. Scientists may use this information to develop new ways to interfere with the bacteria's bile-sensing and gut adaptation processes. They may also use the information to screen for existing drugs that block bile sensing and then test as cholera treatments or prevention strategies in clinical trials. New cholera treatment or prevention approaches that don't rely on antibiotics may help public health officials respond to growing numbers of cholera outbreaks and to prevent the spread of antibiotic-resistant bacteria.

Synthesis and Properties of Branched Hydrogenated Nonasilanes and Decasilanes.

Branched higher silicon hydrides Si nH2 n+2 with n > 6 were recently found to be excellent precursors for the liquid phase deposition of silicon films. Herein we report the gram-scale synthesis of the novel nona- and decasilanes (H3Si)3Si(SiH2) nSi(SiH3)3 (2: n = 1, 5: n = 2) from (H3Si)3SiLi and Cl(SiPh2) nCl by a combined salt elimination/dephenylation/hydrogenation approach. Structure elucidation of the target molecules was performed by NMR spectroscopy and X-ray crystallography. 2 and 5 are nonpyrophoric and exhibit a bathochromically shifted UV absorption compared to neopentasilane and the structurally related octasilane (H3Si)3SiSi(SiH3)3. TG-MS analysis elucidated increased decomposition temperatures and decreased ceramic yields for branched hydrosilanes relative to cyclopentasilane. Otherwise, very similar thermal properties were observed for hydrosilane oligomers with linear and branched structures.