The European Commission has cleared, under the EU Merger Regulation, the proposed acquisition of Varian Inc. by Agilent Technologies Inc., both US companies, by way of purchase of shares. The decision is conditional upon the divestment of Agilent's entire micro/portable gas chromatography instrument business and Varian's entire laboratory gas chromatography, triple quadrupole gas chromatography-mass spectrometry and inductively coupled plasma-mass spectrometry instrument businesses. In view of the remedies proposed, the Commission has concluded that the operation would not significantly impede effective competition in the European Economic Area (EEA) or any substantial part of it.
Trace gas spectroscopic detection has drawn much interest in recent years, as it both allows a better understanding of the molecular spectra of weak overtone transitions and in situ non-intrusive sensing of compounds at low concentration. However, recording a broadband spectrum within a very short measurement time and with high sensitivity remains a challenge. Now, scientists at the Max Planck Institute of Quantum Optics have recorded ultrasensitive absorption broadband spectra within tens of microseconds by combining cavity enhancement and frequency comb spectroscopy.
New spectra, obtained with the SPIRE, PACS and HIFI instruments of the European Space Agency’s (ESA) Herschel Space Observatory during the performance verification phase, have been released by ESA and the instrument teams. Taken together with earlier images the observatory is now on the way to demonstrating that the promised imaging and spectroscopic capabilities are being met.
Understanding the extremely fast atomic mechanisms at work when a protein transitions from one shape to another has been an elusive scientific goal for years, but an essential one for elucidating the full range of protein function. How do proteins transition between distinct shapes without unfolding in the process? Until now, this question has been a hypothetical one, approached by computation only rather than experimentation. In a study in Cell (doi: 10.1016/j.cell.2009.11.022), researchers reveal for the first time computationally and experimentally the molecular pathway that a protein takes to cross the energy barrier. The study reports how folded proteins can efficiently change shape while avoiding unfolding, a critical requirement for any protein in the cell.
Bruker BioSpin has installed the world’s first 1000 MHz ultra-high field NMR AVANCE™ spectrometer at the Centre de Resonance Magnétique Nucléaire à Très Hauts Champs (CRMN) in Lyon, France (a joint research unit of CNRS, Ecole Normale Supérieure de Lyon and Université Lyon 1). The AVANCE 1000 system incorporates a 23.5 Tesla superconducting magnet, and offers exciting research opportunities, both to the CRMN and to other French and European scientists who will access this unique facility.
In structural biology, the only technique available to predict the three-dimensional structure of large complex molecules in solution, such as proteins and DNA, is nuclear magnetic resonance (NMR) spectroscopy. To improve the techniques behind these predictions, the “eNMR” project has launched a new initiative. In September’s Nature Methods (doi: 10.1038/nmeth0909-625) the project issued an invitation to the entire biomolecular NMR community to participate in a large scale test of modern computing algorithms. This community-wide “contest” will potentially improve efficiency, reproducibility and reliability of NMR structure determination. eNMR will be using the Enabling Grids for E-sciencE infrastructure to power their analysis.
Page 16 of 18
- Review of nanoscale infrared spectroscopy applications to energy related materials
- From lake ecology to biofuels—applications of Fourier transform infrared spectroscopy to algal research
- Dating fossil teeth by electron paramagnetic resonance: how is that possible?
- The impact of water pollution with chromium and nickel to the food chain
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