How Primary Structure of Related Heptapeptides Affects Their Charge States and Collision-Induced Dissociation as Investigated by Ion Mobility-Mass Spectrometry
Document Type
Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
Date of Award
Spring 2019
Abstract
A series of structurally related heptapeptides was studied using electrospray ionizationion mobility-mass spectrometry (ESI-IM-MS), collision-induced dissociation (CID), and collision cross-section (CCS) to investigate how their primary structure affects their charge statesand formation of sequence-specific CID product ions. The results were analyzed by Masslynx 4.1 and Driftscope 2.0. These studies are important for developing our understanding of how biological molecules behave in the gas-phase environment of the ESI-IM-MS instrument, and how ESI-IM-MS study can be used for investigating the metal-binding and structure of oligopeptides that contain the 2His-2Cys binding motifs of transcription factors, and are potential therapeutics for metal-related diseases. The results indicated that the designed heptapeptides had fewer metal affinities after Histidine or Cystine were replaced by Glycine, and the CCSs were dependent by molecular weight and charge-state.
Advisor
Laurence A. Angel
Subject Categories
Chemistry | Physical Sciences and Mathematics
Recommended Citation
LIN, YU-FU, "How Primary Structure of Related Heptapeptides Affects Their Charge States and Collision-Induced Dissociation as Investigated by Ion Mobility-Mass Spectrometry" (2019). Electronic Theses & Dissertations. 367.
https://digitalcommons.tamuc.edu/etd/367
