Ontology highlight
ABSTRACT:
SUBMITTER: Liutkute M
PROVIDER: S-EPMC7593090 | biostudies-literature | 2020 Oct
REPOSITORIES: biostudies-literature
Liutkute Marija M Maiti Manisankar M Samatova Ekaterina E Enderlein Jörg J Rodnina Marina V MV
eLife 20201027
Nascent polypeptides begin to fold in the constrained space of the ribosomal peptide exit tunnel. Here we use force-profile analysis (FPA) and photo-induced energy-transfer fluorescence correlation spectroscopy (PET-FCS) to show how a small α-helical domain, the N-terminal domain of HemK, folds cotranslationally. Compaction starts vectorially as soon as the first α-helical segments are synthesized. As nascent chain grows, emerging helical segments dock onto each other and continue to rearrange a ...[more]