Abstract
Most biological processes are associated with protein catalysis. Characterizing protein structure, therefore, is crucial for understanding biological function. Mass spectrometry (MS)-based methods have emerged as a pivotal biophysical tool to interrogate protein structures; they can characterize protein-ligand/protein complexes that are refractory to conventional high-resolution means such as X-ray crystallography, Cryo-EM, and nuclear magnetic resonance (NMR) spectroscopy, in part owing to high molecular weight and significant flexibility. The integrated MS-based platform will provide topology and structural information of proteins from sketch to detail; native MS identifies protein complexes’ composition and stoichiometry; hydrogen-deuterium exchange MS (HDX-MS) detects the protein complexes’ dynamic change at the peptide-level and sometimes at the residue-level; protein footprinting coupled with MS pinpoints the binding site at residue-level via irreversible chemical changes. This thesis comprising eight chapters focuses on method development and application of integrated MS-based platform, using examples of metal-binding proteins and integral membrane proteins that illustrate challenges and solutions.
Committee Chair
Michael L. Gross
Committee Members
Jeffrey P. Henderson, John-Stephen Taylor, Meredith Jackrel, Timothy Wencewicz,
Degree
Doctor of Philosophy (PhD)
Author's Department
Chemistry
Document Type
Dissertation
Date of Award
Spring 5-15-2021
Language
English (en)
DOI
https://doi.org/10.7936/hmr2-gt71
Author's ORCID
http://orcid.org/0000-0002-3600-8157
Recommended Citation
Guo, Chunyang, "Integrated Mass Spectrometry-Based Method in Protein Chemistry: Metal-binding Protein and Integral Membrane Protein" (2021). Arts & Sciences Theses and Dissertations. 2420.
The definitive version is available at https://doi.org/10.7936/hmr2-gt71