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Prof. Bush has been named the recipient of the 2017 Arthur F. Findeis Award for Achievements by a Young Analytical Scientist. The Findeis Award is given annually by the American Chemistry Society Division of Analytical Chemistry, to recognize and encourage outstanding contributions to the fields of analytical chemistry by a young analytical scientist. The award will be presented at the 254th ACS National Meeting to be held August 20-24, 2017 in Washington DC. (Link to additional information about the award)
Native-like and Denatured Cytochrome c Ions Yield Cation-to-Anion Proton-Transfer Products with Similar Collision Cross Sections. Kenneth J. Laszlo, John H. Buckner, Eleanor B. Munger, Matthew F. Bush. J. Am. Soc. Mass Spectrom. 2017, in press. (Link)
The relationship between structures of protein ions, their charge states, and their original structures prior to ionization remains challenging to decouple. Here, we use cation-to-anion proton transfer reactions (CAPTR) to reduce the charge states of cytochrome c ions in the gas phase, and ion mobility to probe their structures. Ions were formed using a new temperature-controlled nanoelectrospray ionization source Continue reading
The Bush Lab welcomes Daniele Canzani! Click here to learn more about Daniele.
Effects of drift gas selection on the ambient-temperature, ion mobility mass spectrometry analysis of amino acids. Kimberly L. Davidson and Matthew F. Bush. Anal. Chem. 2017, DOI: 10.1021/acs.analchem.6b04605. (Link)
Ion mobility (IM) separates ions based on their response to an electric field in the presence of a drift gas. Due to its speed and sensitivity, the integration of IM and mass spectrometry (MS) offers many potential advantages for the analysis of small molecules. To determine the effects that drift gas selection has on the information content of IM separations, absolute collision cross sections (Ω) with He, N2, Ar, CO2, and N2O were measured for the 20 common amino acids using low-pressure, ambient-temperature ion mobility experiments performed in a radio-frequency-confining drift cell. Continue reading
Congratulations to Sam Allen, whose article was one of the top 25 most downloaded articles published in the Analyst in 2016. That article is now featured in the Analyst 2016 Most Accessed Articles Collection.
We are fabricating a new instrument for ion mobility mass spectrometry, which was designed by Sam Allen and Rae Eaton. Here is a video of some recent work by the machine shop in UW Department of Chemistry.
The Bush Lab welcomes Julia Greenwald! Click here to learn more about Julia.
Nonspecific Aggregation in Native Electrokinetic Nanoelectrospray Ionization. Kimberly L. Davidson; Derek R. Oberreit; Christopher J. Hogan; Matthew F. Bush. Int. J. Mass Spectrom. 2016, DOI: 10.1016/j.ijms.2016.09.013. (Link)
Native mass spectrometry is widely used to determine the stoichiometries and binding constants of noncovalent interactions in solution. One challenge is that multiple analytes in a single electrospray droplet can aggregate during solvent evaporation, which will bias the distribution of oligomeric states observed during gas-phase measurements. Here, measurements of solution flow rates, electrospray currents, droplet size distributions, and nonspecific aggregation are used in conjunction with Poisson statistics to characterize the factors that control nonspecific aggregation during typical native mass spectrometry experiments. Continue reading
Analysis 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