The Bush Lab is a research group in the Department of Chemistry and the Biological Physics, Structure & Design Program at the University of Washington. Our research focuses on the development and application of mass spectrometry and ion mobility spectrometry techniques to elucidate the structures and assembly of protein complexes and subcellular machines.
- Interested in joining the Bush Lab? Click here.
- Our weekly group meetings are held on Tuesdays at 5:10 PM in CHL 068B.
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
Members of the Bush Lab will present the following talks at American Society for Mass Spectrometry Annual Conference in San Diego (June 3 – 7, 2018):
- Ion Mobility of Proteins in Nitrogen Gas: Effects of Charge State, Charge Distribution, and Structure Characterized using Trajectory Method Calculations. Daniele Canzani; Matthew F, Bush. (MP 407)
- Collision-Induced Unfolding and Dissociation Reveal the Location of Ni(II) Binding in the Dimer of the Alpha-Crystallin Domain of HSPB5. Seoyeon Hong; Matthew F. Bush. (MP 745)
- Memory of the Condensed-Phase in the Gas-Phase: Effects of Solution, Charge, and Energy on Structures of Serum Albumin Ions. Meagan Gadzuk-Shea; Matthew F Bush. (WOB 10:10)
We look forward to seeing everyone in San Diego!
Congratulations to Julia Greenwald, who received the Bruce R. Kowalski Award for Multidisciplinary Research. The award is given to the best lightning talk at the Center for Process Analysis and Control annual meeting.
Congratulations to Rae Eaton, who just received a Graduate Fellowship from the American Chemical Society Division of Analytical Chemistry! This award is sponsored by Agilent Technologies.
Structural characterization of small molecular ions by ion mobility mass spectrometry in nitrogen drift gas: improving the accuracy of trajectory method calculations. Jong Wha Lee, Hyun Hee L. Lee, Kimberly L. Davidson, Matthew F. Bush, Hugh I. Kim. Analyst 2018, in press. (Link)
The investigation of ion structures based on a combination of ion mobility mass spectrometry (IM-MS) experiments and theoretical collision cross section (CCS) calculations has become important to many fields of research. However, the accuracy of current CCS calculations for ions in nitrogen drift gas limits the information content of many experiments. In particular, few studies have evaluated and attempted to improve the theoretical tools for CCS calculation in nitrogen drift gas. In this study, Continue reading
Our research on “Fundamental Interactions Between Petroleum Ions and Gases” was featured in the most recent annual report from the American Chemical Society Petroleum Research Fund. Congratulations to Kim Davidson and Anna Bakhtina!
Collision Cross Sections and Ion Structures: Development of a General Calculation Method via High-quality Ion Mobility Measurements and Theoretical Modeling. Jong Wha Lee, Kimberly L. Davidson, Matthew F. Bush, Hugh I. Kim. Analyst 2017, in press. (Link)
Ion mobility mass spectrometry (IM-MS) has become an important tool for the structural investigation of ions in the gas phase. Accurate theoretical evaluation of ion collision cross sections (CCSs) is essential for the effective application of IM-MS in structural studies. However, current theoretical tools have limitations in accurately describing a broad range of ions from small molecules to macromolecules. Continue reading
The Bush Lab welcomes Misa! Click here to learn more about Misa.
Congratulations to Kim Davidson, whose research is featured on the cover of the special issue on “New developments and applications of mass spectrometry methods for studying non-covalent protein interactions”.
Nonspecific Aggregation in Native Electrokinetic Nanoelectrospray Ionization. Kimberly L. Davidson; Derek R. Oberreit; Christopher J. Hogan; Matthew F. Bush. Int. J. Mass Spectrom. 2017, 420, 35–42. (Link | Cover)
Effects of Charge State, Charge Distribution, and Structure on the Ion Mobility of Protein Ions in Helium Gas: Results from Trajectory Method Calculations. Kenneth J. Laszlo, Matthew F. Bush. J. Phys. Chem. A, 2017, in press. (Link)
Collision cross section (Ω) values of gas-phase ions of proteins and protein complexes are used to probe the structures of the corresponding species in solution. Ions of many proteins exhibit increasing Ω-values with increasing charge state but most Ω-values calculated for protein ions have used simple collision models that do not explicitly account for charge. Here we use a combination of ion mobility mass spectrometry experiments with helium gas and trajectory method calculations to characterize the extents to which increases in experimental Ω-values with increasing charge state may be attributed to increased momentum transfer concomitant with enhanced long-range interactions between the protein ion and helium atoms. Continue reading