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

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
18 Mar 2024
Accepted
13 May 2024
First published
13 May 2024
This article is Open Access
Creative Commons BY license

Chem. Commun., 2024, Advance Article

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

C. G. L. Veale, A. Chakraborty, R. Mhlanga, F. Albericio, B. G. de la Torre, A. L. Edkins and D. J. Clarke, Chem. Commun., 2024, Advance Article , DOI: 10.1039/D4CC01251H

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