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A Native Mass Spectrometry Approach to Qualitatively Elucidate Interfacial Epitopes of Transient Protein-Protein Interactions

18 April 2024, Version 1
Working Paper
This content is a preprint and has not undergone peer review at the time of posting.

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.

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Version History

Apr 18, 2024 Version 1

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv-2024-pfh2g
D O I: 10.26434/chemrxiv-2024-pfh2g [opens in a new tab]

Funding

Biotechnology and Biological Sciences Research Council
BB/R013993/1
University of Cape Town
Rhodes University
National Research Foundation
98566, 129262
Royal Society
FLAIR

Author’s competing interest statement

The author(s) have declared they have no conflict of interest with regard to this content

Ethics

The author(s) have declared ethics committee/IRB approval is not relevant to this content

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