Structural Origins of FRET-Observed Nascent Chain Compaction on the Ribosome.

ABSTRACT: A fluorescence signal arising from a Förster resonance energy transfer process was used to monitor conformational changes of a domain within the E. coli protein HemK during its synthesis by the ribosome. An increase in fluorescence was observed to begin 10 s after translation was initiated, indicating the domain became more compact in size. Since fluorescence only reports a single value at each time point it contains very little information about the structural ensemble that gives rise to it. Here, we supplement this experimental information with coarse-grained simulations that describe protein conformations and transitions at a spatial resolution of 3.8 Å. We use these simulations to test three hypotheses that might explain the cause of domain compaction: (1) that poor solvent quality con

SUBMITTER: Nissley DA 

PROVIDER: S-EPMC11260357 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature