Chemical cross-linking of interacting proteins locks them in place, and when combined with MS based proteomics, facilitates the identification of tertiary and quaternary structural information. This powerful approach allows researchers to better understand how proteins affect biological processes such as complex formation, signal transduction and enzymatic regulation, as nearly all protein functions are a consequence of their interactions.
Using IonOpticks Aurora Series columns, Steigenberger et al. at Utrecht University demonstrate the advantages of using trapped ion mobility to separate the inherent differences in collisional cross sectional area of mono-linked and cross-linked peptides. This exclusion of peptides with limited cross-linking information led to a substantial increase in detected cross-linked peptides.
Read the full paper
Benefits of Collisional Cross Section Assisted Precursor Selection (caps-PASEF) for Cross-linking Mass Spectrometry.
bioRxiv. 2020 Apr 18. doi: https://doi.org/10.1101/2020.04.16.044859
Steigenberger B, van den Toorn H, Bijl E, Greisch JF, Räther O, Lubeck M, Pieters RJ, Heck A, Scheltema R.
Commentary by Andrew Webb, PhD.
About the author
Andrew has over 15 years’ experience in the field of chromatography and mass spectrometry. He is the lead innovator and inventor at IonOpticks, working closely with the team to test, refine and develop cutting edge techniques to support higher quality outputs and analytics from MS instruments. Andrew is also the Lab Head of the Walter and Eliza Hall Institute of Medical Research’s Proteomics Research Laboratory.