A native mass spectrometry approach to qualitatively elucidate interfacial epitopes of transient protein-protein interactions.
Clinton G L VealeAbir ChakrabortyRichwell MhlangaFernando AlbericioBeatriz G de la TorreAdrienne L EdkinsDavid James ClarkPublished in: Chemical communications (Cambridge, England) (2024)
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.
Keyphrases
- cerebral ischemia
- mass spectrometry
- ionic liquid
- molecular dynamics simulations
- protein protein
- liquid chromatography
- heat shock protein
- electron transfer
- systematic review
- subarachnoid hemorrhage
- high resolution
- perovskite solar cells
- small molecule
- heat stress
- heat shock
- blood brain barrier
- capillary electrophoresis
- brain injury
- high performance liquid chromatography
- oxidative stress
- human immunodeficiency virus
- gas chromatography
- hepatitis c virus
- amino acid
- hiv infected
- antiretroviral therapy