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Assistant Professor
Ph.D., Purdue University
Organic and Biological Mass Spectrometry
Information As a powerful analytical technology, mass spectrometry plays a significant role in the chemical and life sciences. Specifically, my research interests focus on using mass spectrometry at the interface between analytical chemistry, physical organic chemistry, biology and material science. The goal of these projects is to tackle some challenging problems related to chemistry by making use of mass spectrometry. These on-going projects include:
1. Study of ion chemistry and its novel application to bioanalytical chemistry using ambient mass spectrometry.
A recent innovation in the field is the advent of ambient mass spectrometry (e.g. desorption electrospray ionization DESI) which is capable of recording mass spectra on ordinary samples, in their native environment, without sample preparation. Our effort will be devoted to the development novel methodologies for selective biomolecule detection in complex matrices based on newly uncovered ion chemistry. In addition, other projects relying on ion chemistry such as chiral recognition, reaction mechanism elucidation and chemical modification of nanomaterials/surfaces will be also conducted.
2. Analytical applications of ambient ion thermal dissociation in proteomics.
Activation and dissociation of gas-phase ions forms the basis for tandem mass spectrometry. The fragmentation of peptide/protein ions is a central topic in proteomics and there is strong interest in novel dissociation methods. Recently, an ambient ion thermal dissociation method has been established which allows the isolation and re-ionization of neutral fragments of peptide/protein ions at atmospheric pressure outside of the mass spectrometer. We are currently interested in the integration of this method into the collection of techniques available to proteomics.
3. Protein footprinting using fast photolytic oxidation of protein (FPOP) method with various oxidants.
Chemical footprinting of proteins has long been proved to be an efficient method for probing protein-protein interactions. FPOP achieves protein oxidation on a microsecond timescale, making it a strong candidate for protein footprinting. The objective of this project is to develop new FPOP methods with novel laser-generated oxidative chemical probes.
Center for Intelligent Chemical Instrumentation (CICI)
Selected Publications 1. Hao Chen, Livia S. Eberlin, R. Graham Cooks, "Neutral Fragment Mass Spectra via Ambient Thermal Dissociation of Peptide/Protein Ions", J. Am. Chem. Soc., 2007, 129, 5880-5886.
2. Hao Chen, Zheng Ouyang, R. Graham Cooks, "Thermal Production and Reactions of Organic Ions at Atmospheric Pressure", Angew. Chem. Int. Ed., 2006, 3656-3660.
3. R. Graham Cooks, Hao Chen, Marcos N. Eberlin, Xubin Zheng and W. Andy Tao, “Polar Acetalization and Transacetalization in the Gas Phase: The Eberlin Reaction”, Chem. Rev. 2006, 106, 188-211.
4. Hao Chen, Ismael Cotte-Rodriguez and R. Graham Cooks, “cis-Diol Functional Group Recognition by Reactive Desorption Electrospray Ionization”, Chem. Commun. 2006, 597-599.
5. Hao Chen, Dina R. Justes and R. Graham Cooks, “Proton Affinities of N-Heterocyclic Carbene Super Bases”, Org. Lett. 2005, 7, 3949-3952.
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