If we missed you during US HUPO in Charleston, South Carolina, this past February, please be sure to visit our Poster Hall and download the latest information around the entire timsTOF family including our timsTOF Pro 2, timsTOF SCP and timsTOF fleX mass spectrometers. The timsTOF family is best-in-class for proteomics, single cell, spatialOMx, imaging and multi-Omic applications.
Please watch our pre-presentation on 4D-Proteomics™ with PaSER™.
Also watch on-demand our presentation from Dr. Ben Orsburn, one of our guest speakers during our lunch seminar held Monday, February 28th.
Lunch Seminar Title: Precision Medicine, Single Cell Proteomics and Real-time Bioinformatics
Location: Crystal D room at the Charleston Marriott, 170 Lockwood Blvd, Charleston, SC 29403.
Jenny Van Eyk, Ph.D.
Erika Glazer Chair in Women's Heart Health, the Director of Advanced Clinical Biosystems Institute in the Department of Biomedical Sciences, the Director of Basic Science Research in the Women's Heart Center, Professor in Medicine and in Biomedical Sciences at Cedars-Sinai, Los Angeles, CA
Chris Adams, Ph.D., Global Business Development Director Bioinformatics, Life Science Mass Spectrometry, Bruker Daltonics, Billerica, MA, USA
Ben Orsburn, Ph.D.
Research Faculty at The Johns Hopkins University School of Medicine, Baltimore, MD
Posters are available for download:
Christopher Adams, Robin Park, Sven Brehmer, Tharan Srikumar, Jonathan Krieger
Data independent acquisition has become the go to method for deep and quantitative proteomic analysis given the ability to sample large m/z windows in a reproducible and non-stochastic manner. Using a method termed dia-PASEF on a TIMS enabled Q-TOF lends additional advantages in both duty cycle and selectivity using the ion mobility space. Dia-PASEF allows for deep proteomes in short gradient times (<20 min.) and therefore 100’s of LCMS runs can be generated in short times. Data analysis in a streamlined automated fashion expedites the time from experiments to discovery. DIA-NN is a novel software package that uses neural networks providing best-in-class DIA output. Here we integrate DIA-NN onto the PaSER platform for a streamlined workflow for the analysis of many samples in a short analysis time with no file transfer or data migration.
Joanna Bons, Jacob Rose, Christopher Adams, Francesco Pingitore, Birgit Schilling
Protein succinylation is an unexplored PTM and thought to have dramatic consequences on protein structure and thereby function given the large size of the succinyl moiety (100 Da) and amino acid site selectivity (K) changing charge from +1 to -1. In this study, we combine succinylated peptide-level enrichment with timsTOF technology (DDA and DIA) to both identify sites of lysine succinylation and measure changes in succinylation upon dietary treatment in mouse liver tissues.
Philipp Strohmidel, Sebastian Wehner, Jens Decker, Ignacio Jauregui, Christopher Adams, Tharan Srikumar, Sven Brehmer
The PASEF® acquisition mode of the timsTOF Pro has the power to isolate co-eluting, quasi-isobaric peptides separately for fragmentation, based on differences in the peptide’s ion mobility. Such an event is called Mobility Offset Mass Aligned (MOMA) and results in non-chimeric spectra, despite a quadrupoles fidelity. This is especially valuable for PTM analysis, for example to resolve positional isomers of phosphopeptides. TIMS Viz was introduced in PaSER to visualize MOMA events in complex samples.
During acquisition, the MS/MS spectra are streamed to a GPU-powered processing computer performing a real-time database search, called PaSER. The database search utilizes all four dimensions – retention time, CCS value, m/z and fragment spectra – to increase confidence in the identification results. TIMS Viz, a novel data visualization tool to display an interactive heatmap in the m/z ion mobility space, maps MOMA features. Herein, we show the number of MOMA groups, which are sets of at least two MOMA features, that could be identified by TIMS Viz in two different data sets with different m/z tolerance settings. Setting tolerances to 500 mDa (typical lower limits of quadrupole isolation) and a retention time window of 10 s resulted in more than 40,000 MOMA groups containing more than 90,000 spectra for both, the cell lysate sample and the phosphopeptide enriched sample. Without the power of ion mobility separation these spectra would likely be chimeric in nature. Lowering the m/z tolerance to 25 mDa (well below the tolerance of any quadrupole) still leads to more than 18,000 MOMA groups (> 40,000 spectra) for the cell lysate and more than 23,000 MOMA groups (> 52,000 spectra) for the phosphopeptide enriched sample. TIMS Viz helps user to explore their data for MOMA features and is a powerful demonstration how the TIMS dimension can improve the spectral quality for co-eluting, quasi-isobaric peptides.
For Research Use Only. Not for use in clinical diagnostic procedures.