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Article: Effects of Domain Dissection on the Folding and Stability of the 43 kDa Protein PGK Probed by NMR

TitleEffects of Domain Dissection on the Folding and Stability of the 43 kDa Protein PGK Probed by NMR
Authors
Issue Date2003
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmb
Citation
Journal Of Molecular Biology, 2003, v. 330 n. 5, p. 1189-1201 How to Cite?
AbstractThe characterization of early folding intermediates is key to understanding the protein folding process. Previous studies of the N-domain of phosphoglycerate kinase (PGK) from Bacillus stearothermophilus combined equilibrium amide exchange data with a kinetic model derived from stopped-flow kinetics. Together, these implied the rapid formation of an intermediate with extensive native-like hydrogen bonding. However, there was an absence of protection in the region proximal to the C-domain in the intact protein. We now report data for the intact PGK molecule, which at 394 residues constitutes a major extension to the protein size for which such data can be acquired. The methods utilised to achieve the backbone assignment are described in detail, including a semi-automated protocol based on a simulated annealing Monte Carlo technique. A substantial increase in the stability of the contact region is observed, allowing protection to be inferred on both faces of the β-sheet in the intermediate. Thus, the entire N-domain acts concertedly in the formation of the kinetic refolding intermediate rather than there existing a distinct local folding nucleus. © 2003 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/157362
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorReed, MACen_US
dc.contributor.authorHounslow, AMen_US
dc.contributor.authorSze, KHen_US
dc.contributor.authorBarsukov, IGen_US
dc.contributor.authorHosszu, LLPen_US
dc.contributor.authorClarke, ARen_US
dc.contributor.authorCraven, CJen_US
dc.contributor.authorWaltho, JPen_US
dc.date.accessioned2012-08-08T08:49:20Z-
dc.date.available2012-08-08T08:49:20Z-
dc.date.issued2003en_US
dc.identifier.citationJournal Of Molecular Biology, 2003, v. 330 n. 5, p. 1189-1201en_US
dc.identifier.issn0022-2836en_US
dc.identifier.urihttp://hdl.handle.net/10722/157362-
dc.description.abstractThe characterization of early folding intermediates is key to understanding the protein folding process. Previous studies of the N-domain of phosphoglycerate kinase (PGK) from Bacillus stearothermophilus combined equilibrium amide exchange data with a kinetic model derived from stopped-flow kinetics. Together, these implied the rapid formation of an intermediate with extensive native-like hydrogen bonding. However, there was an absence of protection in the region proximal to the C-domain in the intact protein. We now report data for the intact PGK molecule, which at 394 residues constitutes a major extension to the protein size for which such data can be acquired. The methods utilised to achieve the backbone assignment are described in detail, including a semi-automated protocol based on a simulated annealing Monte Carlo technique. A substantial increase in the stability of the contact region is observed, allowing protection to be inferred on both faces of the β-sheet in the intermediate. Thus, the entire N-domain acts concertedly in the formation of the kinetic refolding intermediate rather than there existing a distinct local folding nucleus. © 2003 Elsevier Ltd. All rights reserved.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmben_US
dc.relation.ispartofJournal of Molecular Biologyen_US
dc.subject.meshAlgorithmsen_US
dc.subject.meshComputer Simulationen_US
dc.subject.meshGeobacillus Stearothermophilus - Enzymologyen_US
dc.subject.meshHydrogen Bondingen_US
dc.subject.meshKineticsen_US
dc.subject.meshMagnetic Resonance Spectroscopyen_US
dc.subject.meshMonte Carlo Methoden_US
dc.subject.meshPhosphoglycerate Kinase - Chemistryen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Foldingen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.titleEffects of Domain Dissection on the Folding and Stability of the 43 kDa Protein PGK Probed by NMRen_US
dc.typeArticleen_US
dc.identifier.emailSze, KH:khsze@hku.hken_US
dc.identifier.authoritySze, KH=rp00785en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0022-2836(03)00625-9en_US
dc.identifier.pmid12860138-
dc.identifier.scopuseid_2-s2.0-0038351770en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0038351770&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume330en_US
dc.identifier.issue5en_US
dc.identifier.spage1189en_US
dc.identifier.epage1201en_US
dc.identifier.isiWOS:000184299000024-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridReed, MAC=12646876600en_US
dc.identifier.scopusauthoridHounslow, AM=6602158506en_US
dc.identifier.scopusauthoridSze, KH=7006735061en_US
dc.identifier.scopusauthoridBarsukov, IG=35578733000en_US
dc.identifier.scopusauthoridHosszu, LLP=6603135280en_US
dc.identifier.scopusauthoridClarke, AR=7403682319en_US
dc.identifier.scopusauthoridCraven, CJ=7006100673en_US
dc.identifier.scopusauthoridWaltho, JP=7004600415en_US

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