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New Publication: Analysis of Native-Like Ions Using Structures for Lossless Ion Manipulations

slim_tocAnalysis of Native-Like Ions using Structures for Lossless Ion Manipulations.
Samuel J. Allen, Rachel M. Eaton, and Matthew F. Bush.
Anal. Chem. 2016, DOI: 10.1021/acs.analchem.6b02089. (Link)

Ion mobility separation of native-like protein and protein complex ions expands the structural information available through native mass spectrometry analysis. Here, we implement Structures for Lossless Ion Manipulations (SLIM) for the analysis of native-like ions. SLIM has been shown previously to operate with near lossless transmission of ions up to 3000 Da in mass. Here for the first time, SLIM was used to separate native-like protein and protein complex ions ranging in mass from 12 to 145 kDa. The resulting arrival-time distributions were monomodal and were used to determine collision cross section values that are within 3% of those determined from radio-frequency-confining drift cell measurements. These results are consistent with the retention of native-like ion structures throughout these experiments. Continue reading “New Publication: Analysis of Native-Like Ions Using Structures for Lossless Ion Manipulations”

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2016 Chemistry Awards Dinner

awards_dinner

Congratulations to (from left):

  • Sam Allen, who received a graduate student fellowship from the Irving and Mildred Shain Endowed Fund in Chemistry
  • Kim Davidson, who received a graduate student fellowship from the Reinhardt Family Endowed Fund in Chemistry
  • Rae Eaton, who received a Pacific Northwest National Laboratory Graduate Fellowship and a National Science Foundation Graduate Research Fellowship
  • Cece Hong, who received a graduate student fellowship from the Schomaker Endowed Fund in Chemistry
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Advancing Mass Spectrometry for Biophysics and Structural Biology 2017

iconAMS 2017 will be held at the University of Michigan from July 27th to August 1st. We look forward to seeing everyone in Ann Arbor!

Understanding the global biomolecular structure space is an unquestionably important goal for endeavors ranging from the development of new biomaterials to the diagnosis and treatment of human disease. This conference will bring together a wide array of experts that aim to both develop and apply new mass spectrometry (MS) methods in structural biology and biophysics, broadly defined. The timeliness of this conference coincides with the rapidly expanding role of MS in structural biology, which has already made great strides in extracting the details of biomolecule structures from mixtures, using orders of magnitude less sample than other structural probes. Advancing Mass Spectrometry for Biophysics and Structural Biology 2017 will showcase the best science and promote an exchange of ideas between leaders and new-comers to the biology/mass spectrometry interface, in order to propel this exciting topic toward future successes.

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New Publication: Ion mobility mass spectrometry of peptide, protein, and protein complex ions using a radio-frequency confining drift cell

GAIon mobility mass spectrometry of peptide, protein, and protein complex ions using a radio-frequency confining drift cell
Samuel J. Allen, Kevin Giles, Tony Gilbert, Matthew F. Bush. Analyst 2016, in press. (Link)

Ion mobility mass spectrometry experiments enable the characterization of mass, assembly, and shape of biological molecules and assemblies. Here, a new radio-frequency confining drift cell is characterized and used to measure the mobilities of peptide, protein, and protein complex ions. Continue reading “New Publication: Ion mobility mass spectrometry of peptide, protein, and protein complex ions using a radio-frequency confining drift cell”