Counterfeiting of drugs is a huge industry with an annual turnover of more than €50 billion. In Africa the situation is extremely serious: half of the malaria medication sold there could be ineffective or even harmful. Researchers from Lund University, Sweden, and King’s College London, UK, have now developed a technique based on nuclear magnetic resonance (NMR) that could provide a good way to identify counterfeit drugs.

Magnetic Resonance Spectroscopy can distinguish between neurological diseases in patients without clear symptoms.

Microscopy with atomic resolution could be useful in the determining the structure of some unknown organic compounds, such as medicinally important natural products, according to a study online in Nature Chemistry. This method could avoid the lengthy and expensive process of trying to synthesise the compound and then compare its structure with that of the natural one, which is necessary in some cases.

The new Jean Jeener Bio-NMR Centre at the VIB Department of Molecular and Cellular Interactions, Vrije Universiteit Brussel, has already played a role in a scientific breakthrough that has been published Cell. Thanks to NMR, it is possible to determine the dynamic structure of proteins, and it was used to find out how the activity of certain proteins involved in the stress physiology of bacteria is regulated.

Bio-Rad Laboratories has announced the availability of several new spectral databases.

Bruker has launched its Ascend series of compact, high-field NMR magnets to make high-field NMR more powerful and at the same time more convenient and accessible for NMR laboratories.

Bruker BioSpin has introduced the new Fourier 300, an easy-to-use 300 MHz high-resolution spectrometer that brings FT-NMR within any chemist’s reach. With its robust Fourier probe technology, easy software, miniaturised electronics and proven magnets, it is a complete proton and carbon 1D and 2D FT-NMR system.

The recipients of the 2010 European Magnetic Resonance Awards are John R. Griffiths (Basic Sciences) for his contributions to the applications of magnetic resonance spectroscopy in oncology, and Stefan Neubauer (Medical Sciences) for his contributions to anatomical and functional cardiovascular magnetic resonance imaging and spectroscopy.

Scientists from the Helmholtz Zentrum München and the Technische Universität München (TUM) under the direction of Professor Michael Sattler have developed a new strategy allowing them to determine the spatial structure of biomolecules in solution based around NMR spectroscopy. The method is flexible and generally applicable to obtaining structural information for signal forwarding pathways in the cell or in the regulation of gene expression. Their work is reported in Angewandte Chemie.

Magnetic resonance (MR) spectroscopy may in the future be able both to pinpoint the precise location of prostate cancer and to determine the tumour's aggressiveness, information that could help guide treatment planning. In Science Translational Medicine (doi: 10.1126/scitranslmed.3000513), Massachusetts General Hospital (MGH) researchers report how spectroscopic analysis of the biochemical makeup of prostate glands accurately identified the location of tissue confirmed to be malignant by conventional pathology.

Press release from Nature News - under embargo for Monday 14 December 1800 London time (GMT) Chemical fingerprints of tissue samples taken from patients during operations could soon help surgeons to decide quickly where to make their incisions. Nature News has reported that two groups are leading efforts to use nuclear magnetic resonance (NMR) spectroscopy to analyse the metabolites in biopsies and relay information back to theatre within minutes.

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.

With the addition of the new Sadtler HNMR Chemical Shifts database from Bio-Rad, HaveItAll NMR now includes chemical shift data of 20,391 more compounds, each being identified by chemical name, solvent used in the analysis, instrument name, chemical structure, molecular formula and molecular weight.

The NMR Metabolites database from Bio-Rad, with its collection of 1H and 13C NMR spectra, now includes 532 compounds with 1055 spectra from BioMagResBank data, which doubles the number of spectra previously in this collection of proteins, peptides and nucleic acids.

David Carteau, Isabelle Pianet and Dario M. BassaniInstitut des Sciences Moléculaires, CNRS UMR 5255, Université Bordeaux 1, 351 Cours de la Libération, 33405 Talence France. E-mail: d.bassani@ism.u-bordeaux1.fr

Introduction

Memories of summer vacations on the Mediterranean would not be complete without recollections of the refreshing anise-flavoured alcoholic beverages served during the hot afternoons. Though varying in name and composition across cultures (Raki in Turkey, Arak in Lebanon, Ouzo in Greece, Sambuca in Italy and Pastis in France), extracts from star anis (Illicium floridanum) are a common principal ingredient of the plant extracts used in their production. Besides their pungent anis aroma, another well-known trademark of these drinks is their transition from a clear solution to an opalescent milky-white substance when they are diluted with water. This sudden change in physical appearance will not go unnoticed by a scientist, who may summarily assign it to the precipitation or separation of the hydrophobic organic fragrances due to the addition of water. We know this not to be entirely correct,1 however, as it should lead to a rather un-appetising biphasic mixture in which the essential oils would float on top of a large volume of water and alcohol. The truth behind this apparently simple phenomenon is actually much more complex—and very interesting indeed!

Isotopically-labelled non-radioactive peptides function as critical internal standards for protein quantitation experiments in MS and NMR experiments. Thermo Fisher Scientific now offers multiple grates of heavy peptides, enabling researchers to match the precision and cost of the internal standard according the assay development stage. The new HeavyPeptide Aqua Ultimate kit is designed for absolute quantification and the Aqua Quant Pro kit is a more affordable alternative when ultimate precision is not necessary.

Agilent Technologies have signed a definitive agreement to acquire Varian, paying $1.5 billion. As well as adding $1 billion in annual sales to Agilent’s existing $5.8 billion, it significantly expands the range of technologies in Agilent’s portfolio. Varian are particularly strong in NMR, imaging and vacuum technologies, but also can offer a number of atomic and molecular spectroscopies.