The Bush Lab and collaborators will present the following talks and posters at American Society for Mass Spectrometry Annual Conference in San Antonio, TX (June 5-9):
- Evaluating Gas-Phase Folding of Protein Ions Using Cation to Anion Proton Transfer. Kenneth J. Laszlo; Eleanor B. Munger; Stephanie C. Heard; Matthew F Bush. (MOB 8:50)
- Amino Acid Separation using Different Drift Gases in an RF-Confining Drift Cell. Kimberly Davidson; Matthew F Bush (MOC 9:30)
- Analysis of Native-Like Protein and Protein Complex Ions using Structures for Lossless Ion Manipulations (SLIM). Samuel J. Allen; Rachel M. Eaton; Matthew F. Bush (TP 448)
Sam Allen and Matt Bush will also participate in the Fundamentals Interest Group workshop titled “Modification of Commercial Instruments for Fundamental Research”, which will be held in Room 302A on Tuesday, June 7.
We look forward to seeing everyone in San Antonio!
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
AMS 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.
The Bush Lab welcomes Meagan Gadzuk-Shea! Click here to learn more about Meagan.
The Bush Lab welcomes Cece Hong! Click here to learn more about Cece.
Prof. Bush will present the following talks this January and February:
- Department of Chemistry, University of Alabama, Tuscaloosa, AL, 2/11/16.
- Department of Chemistry, Florida State University, Tallahassee, FL, 2/4/16.
- Department of Chemistry, University of Florida, Gainesville, FL, 2/3/16.
- Department of Chemistry, University of Oregon, Eugene, OR, 1/25/16.
- Society of Western Analytical Professors (SWAP), University of California, Riverside, CA, 1/29/16.
- Triangle Area Mass Spectrometry Discussion Group, NC, 1/13/16. (Link)
Ion 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
Analysis of Native-Like Proteins and Protein Complexes Using Cation to Anion Proton Transfer Reactions (CAPTR). Kenneth J. Laszlo; Matthew F. Bush. J. Am. Soc. Mass Spectrom. 2015, in press. (Link)
Mass spectra of native-like protein complexes often exhibit narrow charge-state distributions, broad peaks, and contributions from multiple, coexisting species. These factors can make it challenging to interpret those spectra, particularly for mixtures with significant heterogeneity. Here we demonstrate the use of ion/ion proton transfer reactions to reduce the charge states of m/z-selected, native-like ions of proteins and protein complexes, a technique that we refer to as cation to anion proton transfer reactions (CAPTR). We then demonstrate that CAPTR can increase the accuracy of charge state assignments and the resolution of interfering species in native mass spectrometry. The CAPTR product ion spectra for pyruvate kinase exhibit ~30 peaks and enable unambiguous determination of the charge state of each peak, whereas the corresponding precursor spectra exhibit ~6 peaks and the assigned charge states have an uncertainty of ±3%. 15+ bovine serum albumin and 21+ yeast enolase dimer both appear near m/z 4450 and are completely unresolved in a mixture. After a single CAPTR event, the resulting product ions are baseline resolved. The separation of the product ions increases dramatically after each subsequent CAPTR event; 12 events resulted in a 3000-fold improvement in separation relative to the precursor ions. Finally, we introduce a framework for interpreting and predicting the figures of merit for CAPTR experiments. More generally, these results suggest that CAPTR strongly complements other mass spectrometry tools for analyzing proteins and protein complexes, particularly those in mixtures.
Prof. Bush is excited to present the following talks next month:
- Korean Society for Mass Spectrometry Conference, Busan, Korea, 8/20/15.
- POSTECH Ion Chemistry Mini-Symposium, Pohang, Korea, 8/17/15.
- Young Chemists Symposium, IUPAC World Chemistry Congress, Busan, Korea, 8/14/15. (9:40-10:00 in Hall 107)
- New Development in MS Fundamentals and Instrumentation Symposium, IUPAC World Chemistry Congress, Busan, Korea, 8/10/15. (11:35-11:55 in Hall 103)
Prof. Bush thanks the IUPAC-2015 Organizing Committee, the Korean Chemical Society, and the Korean Society for Mass Spectrometry for supporting various parts of this visit.