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

8.9K Views

•

11:04 min

•

September 7th, 2019

DOI :

10.3791/60102-v

September 7th, 2019

•

8,950 Views

Enas N. Yousef¹, Ramakrishna Sesham¹, Jacob W. McCabe¹, Rajpal Vangala¹, Laurence A. Angel¹

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

Capítulos

0:04

Title

0:58

Electrospray-ion Mobility-Mass Spectrometry Analysis

3:02

Analysis of ESI-IM-MS pH Titration Data

6:11

Collision Cross-Sections and Computational Methods

8:30

Results: Reaction Mechanisms and Coordination Sites of the Alternative Methanobactin Complexes

10:00

Conclusion

Transcribir

Ion mobility-mass spectrometry, or IM-MS, identify the various products ions from the pH-dependent redox and methyl binding reaction of peptides. With the molecular modeling of their tertiary structure, metal correlation can be determined. IM-MS c

Inicia sesión o comienza tu prueba gratuita para acceder a este contenido

Resumen

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.

Explorar más videos

Ion Mobility mass Spectrometry

IM MS

Metal Ion Recognition

Redox Activity

Metal Binding Oligopeptides

Alternative Methanobactin