Experimental and theoretical investigation of overall energy deposition in surface-induced unfolding of protein ions.

ABSTRACT: Recent advances in native mass spectrometry have enabled its use to probe the structure of and interactions within biomolecular complexes. Surface-induced dissociation, in which inter- and intramolecular interactions are disrupted following an energetic ion-surface collision, is a method that can directly interrogate the topology of protein complexes. However, a quantitative relationship between the ion kinetic energy at the moment of surface collision and the internal energy deposited into the ion has not yet been established for proteins. The factors affecting energy deposition in surface-induced unfolding (SIU) of protein monomers were investigated and a calibration relating laboratory-frame kinetic energy to internal energy developed. Protein monomers were unfolded by SIU and by collis

SUBMITTER: Donor MT 

PROVIDER: S-EPMC6471915 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature