RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11478866http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11478866http://www.w3.org/2000/01/rdf-schema#comment"The influence of an inserted exogenous independent folding element on the thermodynamics and folding properties of SH3 domain from alpha-spectrin has been investigated by creating a fused form between this small all-beta domain and a stable beta-hairpin (BH19). NMR analysis of synthetic peptides shows that insertion of BH19 nucleates formation of the original natural beta-hairpin (distal loop) that is part of the SH3 folding nucleus. The resulting protein (Bergerac-SHH) is more stable, folds faster and contains an elongated hairpin protruding from the globular domain as determined by 2D-NMR. "Protein engineering" analysis of the inserted region shows that it is folded in the transition state. Interestingly, stabilisation by insertion of the distal loop region results in the appearance of a compact intermediate revealed by a curved chevron plot at low denaturant concentration. This effect is eliminated at low salt concentrations by a single mutation of a hydrophobic residue within BH19 sequence, which is most probably involved in non-native interactions. Local stabilisation by enlargement and reinforcement of the folding nucleus, global compaction by the addition of salt and non-native interactions are shown to contribute to the observed deviation from the two-state behaviour."xsd:string
http://purl.uniprot.org/citations/11478866http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.2001.4738"xsd:string
http://purl.uniprot.org/citations/11478866http://purl.uniprot.org/core/author"Serrano L."xsd:string
http://purl.uniprot.org/citations/11478866http://purl.uniprot.org/core/author"Viguera A.R."xsd:string
http://purl.uniprot.org/citations/11478866http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11478866http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/11478866http://purl.uniprot.org/core/pages"357-371"xsd:string
http://purl.uniprot.org/citations/11478866http://purl.uniprot.org/core/title"Bergerac-SH3: "frustation" induced by stabilizing the folding nucleus."xsd:string
http://purl.uniprot.org/citations/11478866http://purl.uniprot.org/core/volume"311"xsd:string
http://purl.uniprot.org/citations/11478866http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11478866
http://purl.uniprot.org/citations/11478866http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11478866
http://purl.uniprot.org/uniprot/#_P07751-mappedCitation-11478866http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11478866
http://purl.uniprot.org/uniprot/P07751http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11478866