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.
The judicious use of a state-of-the-art imaging method enables researchers to capture structural snapshots of complex molecules as they participate in chemical reactions, revealing the sequence of specific atomic motions that lead to chemical change. It’s thought the approach, described in Nature (doi: 10.1038/nature08527), can be used more widely to improve our understanding of important chemical transformations.
The board of directors of Thermo Fisher Scientific Inc. has appointed Marc N. Casper president, chief executive officer and a director of the company, effective 15 October 2009. Casper currently serves as executive vice president and chief operating officer. This announcement follows the decision of Marijn E. Dekkers to resign as president, chief executive officer and a member of the board, in order to become chief executive officer of Bayer AG.
An interdisciplinary team of researchers has created a new, ultra-sensitive technique to analyse life-sustaining protein molecules. The technique may profoundly change the methodology of biomolecular studies and chart a new path to effective diagnostics and early treatment of complex diseases.Researchers from Boston University and Tufts University near Boston, USA, recently demonstrated an infrared spectroscopy technique that can directly identify the "vibrational fingerprints" of extremely small quantities of proteins, the machinery involved in maintaining living organisms.
Since a failed terrorist attack in 2006, plane passengers have not been able to carry bottles of liquid through security at airports, leaving some parched at the airport and others having expensive toiletries confiscated, but work by a group of physicists in Germany is paving the way to eliminate this necessary nuisance.
For high-precision spectroscopy and structural studies of molecules, short light flashes with lowest possible wavelength, i.e., high photon energy, are required. Currently, x-ray flashes of some attosecond (10–18 s) duration are accessible experimentally. Even shorter pulses with even higher photon energy would improve the temporal and spatial resolution, or would allow for the investigation of even smaller structures, such as for example atomic nuclei. In so-called pump-probe experiments, two light pulses of exactly controllable distance are utilised to observe rapid system changes in slow motion.
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- The impact of water pollution with chromium and nickel to the food chain
- Novel concepts in infrared spectral imaging as a cancer diagnostic tool
- Near infrared hyperspectral imaging for foreign body detection and identification in food processing
- Probing and sorting single cells—the application of a Raman-activated cell sorter
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- Atomic absorption
- Atomic emission
- Ion mobility
- Laser spectroscopy
- Mass spectrometry
- Near infrared
- NMR ESR EPR
- Related equipment
- RMs and standards
- Sample prep
- Separation science
- Surface analysis
- X-ray spectrometry