Phosphate Transfer in Activated Protein Complexes Reveals Interaction Sites

Sem Tamara, Richard A. Scheltema, Albert J.R. Heck*, Aneika C. Leney

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


For many proteins, phosphorylation regulates their interaction with other biomolecules. Herein, we describe an unexpected phenomenon whereby phosphate groups are transferred non-enzymatically from one interaction partner to the other within a binding interface upon activation in the gas phase. Providing that a high affinity exists between the donor and acceptor sites, this phosphate transfer is very efficient and the phosphate groups only ligate to sites in proximity to the binding region. Consequently, such phosphate-transfer reactions may define with high precision the binding site between a phosphoprotein and its binding partner, as well as reveal that the binding site in this system is retained in the phase transfer from solution to the gas phase.

Original languageEnglish
Pages (from-to)13641-13644
Number of pages4
JournalAngewandte Chemie - International Edition
Issue number44
Early online date24 Sept 2017
Publication statusPublished - 23 Oct 2017


  • native MS
  • phosphorylation
  • Pin1
  • protein–protein interactions
  • proteomics

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry


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