A two-step probing method to compare lysine accessibility across macromolecular complex conformations.

ABSTRACT: Structural models of large and dynamic molecular complexes are appearing in increasing numbers, in large part because of recent technical advances in cryo-electron microscopy. However, the inherent complexity of such biological assemblies comprising dozens of moving parts often limits the resolution of structural models and leaves the puzzle as to how each functional configuration transitions to the next. Orthogonal biochemical information is crucial to understanding the molecular interactions that drive those rearrangements. We present a two-step method for chemical probing detected by tandem mass-spectrometry to globally assess the reactivity of lysine residues within purified macromolecular complexes. Because lysine side chains often balance the negative charge of RNA in ribonucleoprote

SUBMITTER: MacRae AJ 

PROVIDER: S-EPMC6779377 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature