2011
Chapter Fifteen Probing Serpin Conformational Change Using Mass Spectrometry and Related Methods
Tsutsui Y, Sarkar A, Wintrode P. Chapter Fifteen Probing Serpin Conformational Change Using Mass Spectrometry and Related Methods. Methods In Enzymology 2011, 501: 325-350. PMID: 22078541, PMCID: PMC3679668, DOI: 10.1016/b978-0-12-385950-1.00015-8.Peer-Reviewed Original ResearchConceptsStructural mass spectrometry techniquesHydrogen/deuterium exchangeMass spectrometry techniquesDeuterium exchangeIon mobility mass spectrometrySpectrometry techniquesMass spectrometryMobility mass spectrometrySerpin polymersConformational flexibilitySerpin functionSerpin polymerizationChemical footprintingConformational changesThermodynamic metastabilitySpectrometryChapter FifteenSerpinsStructural distributionPolymerizationPolymersStabilityMisfoldingInhibitory mechanismFootprinting
2009
Local and Global Effects of a Cavity Filling Mutation in a Metastable Serpin
Sengupta T, Tsutsui Y, Wintrode P. Local and Global Effects of a Cavity Filling Mutation in a Metastable Serpin. Biochemistry 2009, 48: 8233-8240. PMID: 19624115, PMCID: PMC2746415, DOI: 10.1021/bi900342d.Peer-Reviewed Original Research
2008
The Structural Basis of Serpin Polymerization Studied by Hydrogen/Deuterium Exchange and Mass Spectrometry*
Tsutsui Y, Kuri B, Sengupta T, Wintrode P. The Structural Basis of Serpin Polymerization Studied by Hydrogen/Deuterium Exchange and Mass Spectrometry*. Journal Of Biological Chemistry 2008, 283: 30804-30811. PMID: 18794298, PMCID: PMC2576545, DOI: 10.1074/jbc.m804048200.Peer-Reviewed Original Research
2007
Cooperative Unfolding of a Metastable Serpin to a Molten Globule Suggests a Link Between Functional and Folding Energy Landscapes
Tsutsui Y, Wintrode P. Cooperative Unfolding of a Metastable Serpin to a Molten Globule Suggests a Link Between Functional and Folding Energy Landscapes. Journal Of Molecular Biology 2007, 371: 245-255. PMID: 17568610, DOI: 10.1016/j.jmb.2007.05.039.Peer-Reviewed Original ResearchConceptsMutagenesis studiesEquilibrium unfoldingMolten globuleCooperative structural unitDramatic conformational changeMultiple structural domainsNumerous mutagenesis studiesExchange mass spectrometryStable native stateNon-cooperative transitionPrevious mutagenesis studiesMolten globule formHydrogen-deuterium exchangeEquilibrium molten globuleFunctional intermediatesProtease-serpin complexesStructural domainsTarget proteasesConformational changesMetastable SerpinNative stateEquilibrium intermediatesCooperative unfoldingUnfolded stateGlobule formHydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions.
Tsutsui Y, Wintrode P. Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions. Current Medicinal Chemistry 2007, 14: 2344-58. PMID: 17896983, DOI: 10.2174/092986707781745596.Peer-Reviewed Original ResearchMeSH KeywordsDeuteriumDeuterium Exchange MeasurementHydrogenMass SpectrometryMolecular StructureProtein BindingProtein ConformationProteinsConceptsProtein assembliesMolecular basisProtein structureNuclear magnetic resonance spectroscopyHydrogen/deuterium exchangeLarge protein assembliesD exchange processX-ray crystallographyDrugs/inhibitorsDynamics of proteinsBackbone amide hydrogensExchange processMagnetic resonance spectroscopyLocal structural environmentPatho-physiological processesViral capsid structureAmide hydrogensHXMSDeuterium exchangeMass spectrometrySmall sample requirementDrug designHigh-quality crystalsResonance spectroscopyProtein conformation
2006
The Conformational Dynamics of a Metastable Serpin Studied by Hydrogen Exchange and Mass Spectrometry
Tsutsui Y, Liu L, Gershenson A, Wintrode P. The Conformational Dynamics of a Metastable Serpin Studied by Hydrogen Exchange and Mass Spectrometry. Biochemistry 2006, 45: 6561-6569. PMID: 16716066, DOI: 10.1021/bi060431f.Peer-Reviewed Original Research