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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
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JoVE Journal Chemistry
Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

DOI:
10.3791/60102-v

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11:04 min

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September 07, 2019

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, , , ,
1Department of Chemistry,Texas A&M University-Commerce

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

Summary

Automatic Translation

Automatic Translation

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

Keywords: 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

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