A priori intrinsic PTM size parameters for predicting the ion mobilities of modified peptides
Kaszycki, Julia L. Shvartsburg, Alexandre A.
Kaszycki, Julia L.
Shvartsburg, Alexandre A.
Other Names
Location
Time Period
Advisors
Original Date
Digitization Date
Issue Date
2017-02
Type
Article
Genre
Keywords
Ion mobility spectrometry,Peptides,Proteomics,Post-translational modifications
Subjects (LCSH)
Citation
Kaszycki, J.L. & Shvartsburg, A.A. J. Am. Soc. Mass Spectrom. (2017) 28: 294
Abstract
The rising profile of ion mobility spectrometry (IMS) in proteomics has driven the efforts to predict peptide cross-sections. In the simplest approach, these are derived by adding the contributions of all amino acid residues and post-translational modifications (PTMs) defined by their intrinsic size parameters (ISPs). We show that the ISPs for PTMs can be calculated from properties of constituent atoms, and introduce the "impact scores" that govern the shift of cross-sections from the central mass-dependent trend for unmodified peptides. The ISPs and scores tabulated for 100 more common PTMs enable predicting the domains for modified peptides in the IMS/MS space that would guide subproteome investigations.
Table of Contents
Description
Click on the DOI link to access the article (may not be free).
Publisher
Springer International Publishing
Journal
Book Title
Series
Journal of The American Society for Mass Spectrometry;v.28:no.2
Digital Collection
Finding Aid URL
Use and Reproduction
Archival Collection
PubMed ID
DOI
ISSN
1044-0305