Document Detail


The influence and utility of varying field strength for the separation of tryptic peptides by ion mobility-mass spectrometry.
MedLine Citation:
PMID:  15694766     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The influence of field strength on the separation of tryptic peptides by drift tube-based ion mobility-mass spectrometry is reported. Operating the ion mobility drift tube at elevated field strengths (expressed in V cm(-1) torr(-1)) reduces separation times and increases ion transmission efficiencies. Several accounts in the literature suggest that performing ion mobility separation at elevated field strength can change the selectivity of ion separation. To evaluate the field strength dependant selectivity of ion mobility separation, we examined a data set of 65 singly charged tryptic peptide ion signals (mass range 500-2500 m/z) at six different field strengths and four different drift gas compositions (He, N2, Ar, and CH4). Our results clearly illustrate that changing the field strength from low field (15 V cm(-1) torr(-1)) to high field (66 V cm(-1) torr(-1)) does not significantly alter the selectivity or peak capacity of IM-MS. The implications of these results are discussed in the context of separation methodologies that rely on the field strength dependence of ion mobility for separation selectivity, e.g., high-field asymmetric ion mobility spectrometry (FAIMS).
Authors:
Brandon T Ruotolo; John A McLean; Kent J Gillig; David H Russell
Related Documents :
12526006 - Secondary ion and laser ablation mass spectrometry for the quantitative characterizatio...
10679976 - Construction of a new multi-turn time-of-flight mass spectrometer.
18356076 - Time-resolved photodissociation of singly protonated peptides with an arginine at the n...
12366056 - Step edge selection during ion erosion of cu(001).
19732016 - High-temperature tolerance in anhydrobiotic tardigrades is limited by glass transition.
6481636 - Intracellular free magnesium in neurones of helix aspersa measured with ion-selective m...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Journal of the American Society for Mass Spectrometry     Volume:  16     ISSN:  1044-0305     ISO Abbreviation:  J. Am. Soc. Mass Spectrom.     Publication Date:  2005 Feb 
Date Detail:
Created Date:  2005-02-07     Completed Date:  2005-05-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9010412     Medline TA:  J Am Soc Mass Spectrom     Country:  United States    
Other Details:
Languages:  eng     Pagination:  158-65     Citation Subset:  IM    
Affiliation:
Laboratory for Biological Mass Spectrometry, Department of Chemistry, Texas A&M University College Station, Texas 77843, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Cattle
Chickens
Electrochemistry
Horses
Kinetics
Mass Spectrometry / methods*
Molecular Sequence Data
Peptide Fragments / analysis,  chemistry,  isolation & purification*,  metabolism*
Rabbits
Trypsin / metabolism*
Chemical
Reg. No./Substance:
0/Peptide Fragments; EC 3.4.21.4/Trypsin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Multiple charging of poly(propylene glycol) by binary mixtures of cations in electrospray.
Next Document:  Zwitterion formation in gas-phase cyclodextrin complexes.