MARATTO

article · Chemical Communications

A native mass spectrometry approach to qualitatively elucidate interfacial epitopes of transient protein–protein interactions

20242 citationsOpen accessRhodes University

Abstract

Native mass spectrometric analysis of TPR2A and GrpE with unpurified peptides derived from limited proteolysis of their respective PPI partners (HSP90 C-terminus and DnaK) facilitated efficient, qualitative identification of interfacial epitopes involved in transient PPI formation. Application of this approach can assist in elucidating interfaces of currently uncharacterised transient PPIs.

Research topics

  • Mass Spectrometry Techniques and Applications
  • Advanced Proteomics Techniques and Applications
  • Enzyme Structure and Function

Read the original research

This page summarises published work. The authoritative version sits with the publisher.

DOI: 10.1039/d4cc01251h

Is something wrong with this record? Report it or request removal.

Discussion

Discuss this research

Have you built on this work, tried to replicate it, or seen it applied in practice? Share what you know. Verified researchers and MARATTO™ domain experts can open a discussion, and any member can reply. Contributions are reviewed before they appear.

No discussion yet. Open the first thread.