Ontology highlight
ABSTRACT:
SUBMITTER: Elfageih R
PROVIDER: S-EPMC7513700 | biostudies-literature | 2020 Oct
REPOSITORIES: biostudies-literature
Elfageih Rageia R Karyolaimos Alexandros A Kemp Grant G de Gier Jan-Willem JW von Heijne Gunnar G Kudva Renuka R
Protein science : a publication of the Protein Society 20200824 10
Cotranslational protein folding studies using Force Profile Analysis, a method where the SecM translational arrest peptide is used to detect folding-induced forces acting on the nascent polypeptide, have so far been limited mainly to small domains of cytosolic proteins that fold in close proximity to the translating ribosome. In this study, we investigate the cotranslational folding of the periplasmic, disulfide bond-containing Escherichia coli protein alkaline phosphatase (PhoA) in a wild-type ...[more]