Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis.

ABSTRACT: Cotranslational folding (CTF) is a fundamental molecular process that ensures efficient protein biosynthesis and minimizes the formation of misfolded states. However, the complexity of this process makes it extremely challenging to obtain structural characterizations of CTF pathways. Here, we correlate observations of translationally arrested nascent chains with those of a systematic C-terminal truncation strategy. We create a detailed description of chain length-dependent free energy landscapes associated with folding of the FLN5 filamin domain, in isolation and on the ribosome, and thus, quantify a substantial destabilization of the native structure on the ribosome. We identify and characterize two folding intermediates formed in isolation, including a partially folded intermediate assoc

SUBMITTER: Waudby CA 

PROVIDER: S-EPMC6166796 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature