Journal
JOURNAL OF PROTEOME RESEARCH
Volume 10, Issue 5, Pages 2318-2329Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr1011312
Keywords
ion mobility spectrometry; mass spectrometry; peptide identification
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Funding
- National Institutes of Health [1RC1GM090797-01]
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A new method for enhancing peptide ion identification in proteomics analyses using ion mobility data is presented. Ideally, direct comparisons of experimental drift times (t(D)) with a standard mobility database could be used to rank candidate peptide sequence assignments. Such a database would represent only a fraction of sequences in protein databases and significant difficulties associated with the verification of data for constituent peptide ions would exist. A method that employs intrinsic amino acid size parameters to obtain ion mobility predictions that can be used to rank candidate peptide ion assignments is proposed. Intrinsic amino acid size parameter; have been determined for doubly charged peptide ions from an annotated yeast proteome. Predictions of ion mobilities using the intrinsic size parameters are more accurate than those obtained from a polynomial fit to t(D) versus molecular weight data. More than a 2-fold improvement in prediction accuracy has been observed for a group of arginine-terminated peptide ions 12 residues in length. The use of this predictive identification is discussed, and a simple peptide ion scoring scheme is presented.
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