A novel Fourier transform ion cyclotron resonance mass spectrometer with improved ion trapping and detection capabilities.
A novel Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer has been developed for improved biomolecule analysis. A flared metal capillary and an electrodynamic ion funnel were installed in the source region of the instrument for improved ion transmission. The transfer quadrupole is divided into 19 segments, with the capacity for independent control of DC voltage biases for each segment. Restrained ion population transfer (RIPT) is used to transfer ions from the ion accumulation region to the ICR cell. The RIPT ion guide reduces mass discrimination that occurs as a result of time-of-flight effects associated with gated trapping. Increasing the number of applied DC bias voltages from 8 to 18 increases the number of ions that are effectively trapped in the ICR cell. The RIPT ion guide with a novel voltage profile applied during ion transfer provides a 3- to 4-fold increase in the number of ions that are trapped in the ICR cell compared with gated trapping for the same ion accumulation time period. A novel ICR cell was incorporated in the instrument to reduce radial electric field variation for ions with different z-axis oscillation amplitudes. With the ICR cell, called trapping ring electrode cell (TREC), we can tailor the shape of the trapping electric fields to reduce dephasing of coherent cyclotron motion of an excited ion packet. With TREC, nearly an order of magnitude increase in sensitivity is observed. The performance of the instrument with the combination of RIPT, TREC, flared inlet, and ion funnel is presented.
Kaiser
Nathan K
NK
Department of Chemistry, Washington State University, Pullman, Washington 98195-5065, USA.
Skulason
Gunnar E
GE
Weisbrod
Chad R
CR
Bruce
James E
JE
D000818:Animals; D002417:Cattle; D004867:Equipment Design; D005583:Fourier Analysis; D007477:Ions / Q000737:chemistry; D013058:Mass Spectrometry / Q000295:instrumentation*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D012680:Sensitivity and Specificity; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D007477:Ions; D010446:Peptide Fragments; D012710:Serum Albumin, Bovine; D014357:Trypsin