Ontology highlight
ABSTRACT:
SUBMITTER: Hanazono Y
PROVIDER: S-EPMC6070647 | biostudies-literature | 2018 Aug
REPOSITORIES: biostudies-literature
FEBS open bio 20180627 8
Nascent polypeptide chains fold cotranslationally, but the atomic-level details of this process remain unknown. Here, we report crystallographic, <i>de novo</i> modeling, and spectroscopic studies of intermediate-length variants of the λ repressor N-terminal domain. Although the ranges of helical regions of the half-length variant were almost identical to those of the full-length protein, the relative orientations of these helices in the intermediate-length variants differed. Our results suggest ...[more]