http://purl.uniprot.org/citations/30087834 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/30087834 | http://www.w3.org/2000/01/rdf-schema#comment | "Nascent polypeptide chains fold cotranslationally, but the atomic-level details of this process remain unknown. Here, we report crystallographic, de novo 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 that cotranslational folding of the λ repressor initially forms a helical structure with a transient conformation, as in the case of a molten globule state. This conformation subsequently matures during the course of protein synthesis.DatabaseStructural data are available in the PDB under the accession numbers http://www.rcsb.org/pdb/search/structidSearch.do?structureId=5ZCA and http://www.rcsb.org/pdb/search/structidSearch.do?structureId=3WOA."xsd:string |
http://purl.uniprot.org/citations/30087834 | http://purl.org/dc/terms/identifier | "doi:10.1002/2211-5463.12480"xsd:string |
http://purl.uniprot.org/citations/30087834 | http://purl.uniprot.org/core/author | "Takeda K."xsd:string |
http://purl.uniprot.org/citations/30087834 | http://purl.uniprot.org/core/author | "Miki K."xsd:string |
http://purl.uniprot.org/citations/30087834 | http://purl.uniprot.org/core/author | "Hanazono Y."xsd:string |
http://purl.uniprot.org/citations/30087834 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
http://purl.uniprot.org/citations/30087834 | http://purl.uniprot.org/core/name | "FEBS Open Bio"xsd:string |
http://purl.uniprot.org/citations/30087834 | http://purl.uniprot.org/core/pages | "1312-1321"xsd:string |
http://purl.uniprot.org/citations/30087834 | http://purl.uniprot.org/core/title | "Co-translational folding of alpha-helical proteins: structural studies of intermediate-length variants of the lambda repressor."xsd:string |
http://purl.uniprot.org/citations/30087834 | http://purl.uniprot.org/core/volume | "8"xsd:string |
http://purl.uniprot.org/citations/30087834 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/30087834 |
http://purl.uniprot.org/citations/30087834 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/30087834 |
http://purl.uniprot.org/uniprot/#_P0AEX9-mappedCitation-30087834 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/30087834 |
http://purl.uniprot.org/uniprot/#_P03034-mappedCitation-30087834 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/30087834 |
http://purl.uniprot.org/uniprot/P0AEX9 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/30087834 |
http://purl.uniprot.org/uniprot/P03034 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/30087834 |