Cold mass spec

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  • Published: Aug 7, 2014
  • Author: Steve Down
  • Channels: Base Peak / Infrared Spectroscopy / Atomic / NMR Knowledge Base / Chemometrics & Informatics / MRI Spectroscopy / Raman / X-ray Spectrometry / UV/Vis Spectroscopy / Proteomics

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Mass spectra have been recorded by cooling the interface between atmospheric pressure and the vacuum inlet rather than heating it, a technique which could yield spectra from thermally unstable compounds and lightly bound complexes.

This unusual approach has been described by mass spectrometrists in the US writing in Analytical Chemistry. They described how the simple operation of feeding a sample solution into a tube that was cooled by dry ice and connected to the vacuum system produced ions. Spectra were observed for peptides and proteins, as well as small molecules like tetrabutylammonium iodide.

The ionisation mechanism was likened to that occurring in thunderclouds, when charge separation occurs to generate ions. In this case, the researcher suggested that charged droplets or particles were created during charge separation under cold conditions and were protected by a solvent cage, bare ions being seen after desolvation.

Using this fledgling technique, mass spectra were recorded for myoglobin in cooled methanol and the largest protein observed so far from freezing water was ubiquitin. However, major problems remain to be resolved, particularly clogging of the inlet by ice.


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