Randall seminar: Using mass spectrometry to examine disordered proteins – the perfect tool to report on self solvation and complex formation?

Speaker:  Professor Perdita Barran, Manchester Institute of Biotechnology, University of Manchester

Using mass spectrometry to examine disordered proteins – the perfect tool to report on self solvation and complex formation?

Host: Franca Fraternali

Abstract: In the last ten years mass spectrometry (MS) coupled with electrospray ionisation (ESI) has been extensively applied to identify proteins and elucidate stoichiometry of protein complexes, often without the need for labels. Because desolvated species are affected by solvent conditions such as pH, buffer strength and concentration, ESI-MS is an appropriate method by which to consider the range of conformational states that proteins may occupy including natively folded, disordered, denatured and amyloid.

Rotationally averaged collision cross sections of the ionised forms of proteins, provided by the combination of mass spectrometry and ion mobility (IM-MS), are also instructive in exploring conformational landscapes in the absence of solvent. The mass and conformer selected ions can also be subjected to dissociation (CAD, ECD, SID, UVPD) which can delineate the structure further. 

This presentation will discuss recent results in this area.