Laboratory for Biological Mass Spectrometry (LBMS)

IU Bloomington

Jonathan Trinidad

https://bmslab.sitehost.iu.edu/index.html

The LBMS is broadly interested in the development and application of proteomic techniques that facilitate understanding of biological systems at the molecular level. There is a particular emphasis on several lines of research:

Biochemical approaches to enrich and characterize post-translationally modified (PTM) peptides and proteins. A key aspect of large-scale PTM characterization is the ability to enrich specific classes of modified peptides. Examples include: TiO2 chromatography for the enrichment of phosphopeptides; immobilized lectin chromatography for the enrichment of glycopeptides; anti-acetyllysine antibodies for the enrichment of acetylated peptides; anti-GlyGly remanant antibodies for the enrichment of peptides bearing a ubiquitin attachment sites; biotin-capture and release approaches for enriching persulfidated peptides.

The development and application of large scale techniques that enable quantitative comparisons between cells or tissue in distinct physiological states. We have extensive experience with label-free quantification using the intensity of the top three peptides on a Synapt G2S equipped with ion mobility. We also commonly use stable isotope labeling strategies such as iTRAQ or TMT. Proteomic applications of Ion Mobility Spectrometry, particularly with respect to the previous two research aims.

• IU Proteomics Facility Policies
• IU Proteomics Facility Rates

• protein digestion (in-solution or in-gel)

• nanoLC-MS/MS (ion trap / orbitrap)

• nanoLC(chip-cube)-ETD/MS/MS (ion trap)

• direct infusion MS and MS/MS (ion trap / FTMS) FTMS equipped with CID and ETD

• Jonathan Trinidad : trinidad@indiana.edu 812-856-4126