January 2012
The Federation of Analytical Chemistry and Spectroscopy Societies (FACSS) has announced the winners of the 2011 FACSS Innovations Awards. The FACSS Innovation Awards showcase the newest and most creative science debuted orally at a FACSS-organised conference. Shortlisted finalists competed in front of expert panels at the 2011 FACSS conference in Reno, NV, USA (2–7 October 2011). The panel commended the high quality of entries and selected four equal awardees.
For the past 30 years, one of the most valuable and widely used techniques for studying electronic structures has been Angle-Resolved PhotoEmission Spectroscopy (ARPES). However, this technique primarily looks at surfaces. Now, for the first time, bulk electronic structures have been opened to comparable scrutiny through a new variation of this standard called Hard x-ray Angle-Resolved PhotoEmission Spectroscopy (HARPES).
Researchers have used mass spectrometry imaging to uncover exactly how a human egg captures an incoming sperm to begin the fertilisation process, in a new study published this week in Science. The research identifies the sugar molecule that makes the outer coat of the egg “sticky”, which is vital for enabling the sperm and egg to bind together. Researchers across the world have been trying to understand what performs this task for over 30 years.
Using two-dimensional spectroscopy, researchers in Berlin have shown that electrons in a semiconductor are best described as a cloud with a size of a few nanometres. The cloud size is determined by the interaction of the electron with vibrations in the crystal lattice.
Dr Fiona Lyng of Dublin Institute of Technology is this year’s winner of the Enterprise Ireland “One to Watch” award. Dr Lyng is developing a new system using Raman spectroscopy to diagnose cervical cancer together with her colleagues at the Radiation and Environmental Science Centre at the Focas Institute in DIT and collaborators at the Coombe Women and Infants University Hospital.
A large number of illnesses stem from misfolded proteins, molecules composed of amino acids. Researchers at the University of Zurich, Switzerland, have now studied protein misfolding using a special spectroscopic technique— single-molecule fluorescence. Misfolding, as they report in Nature, is more frequent if the sequence of the amino acids in the neighbouring protein domains is very similar.
Researchers from the Basque nanoscience research center, CIC nanoGUNE, and Neaspec GmbH (Germany) have developed an instrument that allows for recording infrared spectra with a thermal source at a resolution that is 100 times better than in conventional infrared spectroscopy. In future, the technique could be applied for analysing the local chemical composition and structure of nanoscale materials in polymer composites, semiconductor devices, minerals or biological tissue.
A joint cooperation between three research groups at nanoGUNE (Donostia, San Sebastian, Spain) reports an innovative method to focus infrared light with tapered transmission lines to nanometre-size dimensions. This device could trigger the development of novel chemical and biological sensing tools, including ultra-small infrared spectrometers and lab-on-a-chip integrated biosensors.
