Kokic, Goran

[["dc.bibliographiccitation.firstpage","1104"],["dc.bibliographiccitation.issue","6264"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1107"],["dc.bibliographiccitation.volume","350"],["dc.contributor.author","Holtkamp, Wolf"],["dc.contributor.author","Kokic, Goran"],["dc.contributor.author","Jäger, Marcus"],["dc.contributor.author","Mittelstaet, Joerg"],["dc.contributor.author","Komar, Anton A."],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:54:52Z"],["dc.date.available","2017-09-07T11:54:52Z"],["dc.date.issued","2015"],["dc.description.abstract","Protein domains can fold into stable tertiary structures while they are synthesized on the ribosome. We used a high-performance, reconstituted in vitro translation system to investigate the folding of a small five-helix protein domain-the N-terminal domain of Escherichia coli N5-glutamine methyltransferase HemK-in real time. Our observations show that cotranslational folding of the protein, which folds autonomously and rapidly in solution, proceeds through a compact, non-native conformation that forms within the peptide tunnel of the ribosome. The compact state rearranges into a native-like structure immediately after the full domain sequence has emerged from the ribosome. Both folding transitions are rate-limited by translation, allowing for quasi-equilibrium sampling of the conformational space restricted by the ribosome. Cotranslational folding may be typical of small, intrinsically rapidly folding protein domains."],["dc.identifier.doi","10.1126/science.aad0344"],["dc.identifier.gro","3141785"],["dc.identifier.isi","000366422600047"],["dc.identifier.pmid","26612953"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1046"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.title","Cotranslational protein folding on the ribosome monitored in real time"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","833"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","840"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Boehning, Marc"],["dc.contributor.author","Dugast-Darzacq, Claire"],["dc.contributor.author","Rankovic, Marija"],["dc.contributor.author","Hansen, Anders S."],["dc.contributor.author","Yu, Taekyung"],["dc.contributor.author","Marie-Nelly, Herve"],["dc.contributor.author","McSwiggen, David T."],["dc.contributor.author","Kokic, Goran"],["dc.contributor.author","Dailey, Gina M."],["dc.contributor.author","Cramer, Patrick"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2022-03-01T11:46:02Z"],["dc.date.available","2022-03-01T11:46:02Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1038/s41594-018-0112-y"],["dc.identifier.pii","112"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103536"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1545-9985"],["dc.relation.issn","1545-9993"],["dc.rights.uri","http://www.springer.com/tdm"],["dc.title","RNA polymerase II clustering through carboxy-terminal domain phase separation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]