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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
Chapters
- 00:04Title
- 00:58Electrospray-ion Mobility-Mass Spectrometry Analysis
- 03:02Analysis of ESI-IM-MS pH Titration Data
- 06:11Collision Cross-Sections and Computational Methods
- 08:30Results: Reaction Mechanisms and Coordination Sites of the Alternative Methanobactin Complexes
- 10:00Conclusion
Ion mobility-mass spectrometry and molecular modeling techniques can characterize the selective metal chelating performance of designed metal-binding peptides and the copper-binding peptide methanobactin. Developing new classes of metal chelating peptides will help lead to therapeutics for diseases associated with metal ion misbalance.
Tags
Ion Mobility-mass SpectrometryIM-MSMetal Ion RecognitionRedox ActivityMetal Binding OligopeptidesMolecular ModelingTertiary StructureMetal CorrelationESI-IM-MSPoly-DL-alanineAlternative MethanobactinPH-dependent RedoxMethyl Binding ReactionProduct IonsStoichiometryProtonation StateConformational StructureMetal Chelating PeptidesTherapeuticsMenkes DiseaseWilson’s DiseaseCancerAlzheimer’s DiseaseNative ESI-IM-MSNegative IonPositive IonAcetic AcidAmmonium HydroxideMass-to-chargeIsotope Pattern
