Remeasurement of electrosprayed proteins in the trapped ion cell of a Fourier transform ion cyclotron resonance mass spectrometer

Abstract

A single population of multiply charged protein ions formed by electrospray ionization (ESI) is subjected to multiple Fourier transform ion cyclotron resonance (FTICR) excitation and detection events without promoting ion loss from the trapped ion cell. This nondestructive approach to mass spectrometric detection will allow detection limits to be significantly reduced by averaging the repetitive time-domain response that follows each excitation event. Under appropriate conditions, unit remeasurement efficiency is observed for large proteins; for example, 250 consecutive remeasurements of a single population of bovine albumin dimer ions (MW 132,532) yield the expected 16-fold improvement in signal-to-noise ratio compared to a single measurement. Examples presented include a 14-fmol sample of horse myoglobin (MW 16,951), which yields a 15:1 S/N for 50 remeasurements compared to a single scan S/N of 2:1 and a 30-fmol sample of bovine albumin dimer which exhibits a S/N of 25:1 for 50 remeasurements compared to a single scan S/N of 3:1. Of both practical and theoretical interest is the observation of a rapid collision-mediated homogeneous relaxation process that can return these large ions to the center of the cell within a few hundred milliseconds after excitation.