Biophysical Mass Spectrometry at the University of Washington
The Bush Lab was just awarded a grant from the National Institutes of Health for a project titled “Increasing the Selectivity of Hybrid Mass Spectrometry Using Multidimensional Ion Mobility Spectrometry” (R01 GM130708). We are excited to pursue this research and are grateful for this financial support from the NIH.
The Bush Lab is excited to join the eScience Institute, which empowers researchers and students in all fields to answer fundamental questions through the use of large, complex, and noisy data. As the hub of data-intensive discovery on campus, the eScience Institute leads a community of innovators in the techniques, technologies, and best practices of data science and the fields that depend on them.
Snow is rare in Seattle, which makes us appreciate it more than people in most places. Here are some pictures from near our lab.
The Bush Lab welcomes Aditya! Click here to learn more about Aditya.
On August 1st, Rae Eaton, a graduate student in the Bush Lab, presented a talk entitled “Out of the Attic, Into the Lab: building a shrink ray is harder than it looks” The talk was part of the Science and a Movie program, a series put on by Central Cinema and the Pacific Science Center. The series pairs talks from scientists in the Seattle area with silly or classic movies.
In the talk, Rae used stories from the world of bioanalytical chemistry to discuss the challenges home inventors can run into working in unusual spaces, and explores the benefits a lab offers versus working by oneself in their garage. The talk was followed by a screening of “Honey I Shrunk the Kids”.
Thanks to Central Cinema and the Pacific Science Center’s Meet a Scientist program for the opportunity!
The Bush Lab website would like to formally welcome AnneClaire and Ben, who are just finishing their first year in the Bush Lab.
The Bush Lab was just awarded a grant from the National Science Foundation for a project titled “Bridging the Gap Between Observables from Ion Mobility Mass Spectrometry and the Structures of Native Proteins” (1807382). We are excited to pursue this research and are grateful for this financial support from the NSF.
Ion Mobility of Proteins in Nitrogen Gas: Effects of Charge State, Charge Distribution, and Structure. Daniele Canzani, Kenneth J. Laszlo, Matthew F. Bush. J. Phys. Chem. A 2018, in press. (Link)
Ion mobility is emerging as a rapid and sensitive tool for structural characterization. Collision cross-section (Ω) values determined using ion mobility are often compared to values calculated for candidate structures generated through molecular modeling. Several methods exist for calculating Ω values, but the trajectory method explicitly includes contributions from long-range, ion–neutral interactions. Recent implementations of the trajectory method have significantly reduced its expense and have made applications to proteins far more tractable. Here, we use ion mobility experiments and trajectory method calculations to characterize the effects of charge state, charge distribution, and structure on the ion mobility of proteins in nitrogen gas. These results show that ion-induced dipole interactions Continue reading “New Publication: Ion Mobility of Proteins in Nitrogen Gas: Effects of Charge State, Charge Distribution, and Structure”
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