Influence of Crosslinker Identity and Position on Gas-phase Dissociation of Lys-lys Crosslinked Peptides.
From: Sandia National Laboratories, Livermore, California 94551-0969, USA. spgauch@sandia.gov
Journal of the American Society for Mass Spectrometry
- Publish Date: Mar 2006
- ISSN: 1044-0305
- Volume: 17
- Issue: 3
- Pages: 395-405
- Medium: Print
- Language: English
- Citation (JAMA): Gaucher Sara P, Hadi Masood Z, Young Malin M, et al. Influence of Crosslinker Identity and Position on Gas-phase Dissociation of Lys-lys Crosslinked Peptides.. J. Am. Soc. Mass Spectrom. Mar 2006;17:395-405
Abstract
A systematic study of the dissociation patterns of crosslinked peptides analyzed by tandem mass spectrometry is reported. A series of 11-mer peptides was designed around either a polyalanine or polyglycine scaffold with arginine at the C terminus. One or two lysine residues were included at various locations within the peptides to effect inter- or intra-molecular crosslinking, respectively. Crosslinked species were generated with four commonly used amine-specific chemical crosslinking reagents: disuccinimidyl suberate (DSS), disuccinimidyl tartarate (DST), dithiobis(succinimidylpropionate) (DSP), and disuccinimidyl glutarate (DSG). The influence of precursor charge state, location of crosslink, and specific crosslinking reagent on the MS/MS dissociation pattern was examined. Observed trends in the dissociation patterns obtained for these species will allow for improvements to software used in the automated interpretation of crosslinked peptide MS/MS data.
Mesh Headings (Keywords): Binding Sites, Cross-Linking Reagents, Gases, Lysine, Peptides, Phase Transition, Protein Binding, Spectrometry, Mass, Electrospray Ionization
Check for Full Text / PubMed Unique Identifier (PMID): 16443364
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