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.

中文翻译：

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定性阐明瞬时蛋白质-蛋白质相互作用的界面表位的天然质谱方法

使用源自其各自 PPI 伴侣（HSP90 C 末端和 DnaK）有限蛋白水解的未纯化肽对 TPR2A 和 GrpE 进行天然质谱分析，有助于有效、定性地鉴定参与瞬时 PPI 形成的界面表位。应用这种方法可以帮助阐明当前未表征的瞬态 PPI 的界面。