Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR).

ABSTRACT: We describe a high-throughput in-cell nuclear magnetic resonance (NMR)-based method for mapping the structural changes that accompany protein-protein interactions (STINT-NMR). The method entails sequentially expressing two (or more) proteins within a single bacterial cell in a time-controlled manner and monitoring the protein interactions using in-cell NMR spectroscopy. The resulting spectra provide a complete titration of the interaction and define structural details of the interacting surfaces at atomic resolution.

SUBMITTER: Burz DS 

PROVIDER: S-EPMC4447212 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature