Date of Graduation

1999

Document Type

Thesis

Degree Type

MS

College

Eberly College of Arts and Sciences

Department

Chemistry

Committee Chair

Fred L. King

Committee Member

Paul W. Jagodzinski

Committee Member

Ronald B. Smart

Abstract

Electrospray Ionization Mass Spectrometry is gaining recognition as a powerful tool for the study of proteins. It is a “soft” ionization source, which permits the preservation of noncovalent interactions prevailing in biological systems. It is able to form multiply charged ions, which facilitates analyses of very large molecules. The change of the protein conformations can be investigated by charge state distribution shifts in ESI-MS. The noncovalent interactions of proteins with other molecules can also be studied by ESI-MS because these interactions often change the shape of proteins. I examined the effect of various operating parameters on shape of the ESI-MS spectra. Those operating parameters include Source CID, Tube Lens Offset, Flow Rate, and Capillary Temperature. The study shows that the operating parameters do affect the shape of ESI-MS spectra. The spectra can reflect the conformation change only when the operating parameters are carefully controlled. Different effects result from the processes of Electrospray Ionization. The interaction of proteins with metals can also be investigated by ESI-MS. I observed that Ubiquitin interact with various cations with +1 and +2 charge states. The strength of Ubiquitin-metal bonds was investigated by ESI-MS. The order of the relative strength of Ubiquitin-metal bonds was obtained by ESI-MS.

Download

Share

COinS