| http://purl.uniprot.org/citations/26011795 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26011795 | http://www.w3.org/2000/01/rdf-schema#comment | "Native mass spectrometry (MS) methods permit the study of multiple protein species within solution equilibria, whereas ion mobility (IM)-MS can report on conformational behavior of specific states. We used IM-MS to study a conformationally labile protein (α1 -antitrypsin) that undergoes pathological polymerization in the context of point mutations. The folded, native state of the Z-variant remains highly polymerogenic in physiological conditions despite only minor thermodynamic destabilization relative to the wild-type variant. Various data implicate kinetic instability (conformational lability within a native state ensemble) as the basis of Z α1 -antitrypsin polymerogenicity. We show the ability of IM-MS to track such disease-relevant conformational behavior in detail by studying the effects of peptide binding on α1 -antitrypsin conformation and dynamics. IM-MS is, therefore, an ideal platform for the screening of compounds that result in therapeutically beneficial kinetic stabilization of native α1 -antitrypsin. Our findings are confirmed with high-resolution X-ray crystallographic and nuclear magnetic resonance spectroscopic studies of the same event, which together dissect structural changes from dynamic effects caused by peptide binding at a residue-specific level. IM-MS methods, therefore, have great potential for further study of biologically relevant thermodynamic and kinetic instability of proteins and provide rapid and multidimensional characterization of ligand interactions of therapeutic interest."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.org/dc/terms/identifier | "doi:10.1002/pro.2706"xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Christodoulou J."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Day J."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Lomas D.A."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Gooptu B."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Haq I."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Kirkpatrick J."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Irving J.A."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Nyon M.P."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Thalassinos K."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Levy G."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Sivalingam G.N."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/author | "Prentice T."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/name | "Protein Sci"xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/pages | "1301-1312"xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/title | "An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of alpha1 -antitrypsin upon ligand binding."xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://purl.uniprot.org/core/volume | "24"xsd:string |
| http://purl.uniprot.org/citations/26011795 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26011795 |
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| http://purl.uniprot.org/uniprot/#_A0A384MDQ7-mappedCitation-26011795 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26011795 |