MSPIRE REU Program:|
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General Information Page
A U.S.-Netherlands Summer Research Experience for Undergraduates (REU) program is an integral part of the MSPIRE’s educational mission.
The MSPIRE REU program provides training and financial support for U. S. undergraduate students to participate in MSPIRE research projects under the guidance of one of the MSPIRE faculty. See the MSPIRE Faculty and Their Research Interests below.
The program is open to undergraduate Chemistry majors who ideally will graduate in 2015 or 2016, but applications will be accepted from any undergraduate Chemistry major. Priority will be given to applicants that plan on attending graduate school in Chemistry. Minority applicants are encouraged to apply. In addition to completing the on-line application form, a transcript of your undergraduate academic record must be submitted and two letters of recommendations should be provided (on-line) on your behalf from faculty members who are familiar with your recent progress as chemistry major. Prompt application is encouraged, because limited openings are available and applications are considered at frequent intervals.
The summer program runs for 10 weeks between mid May and mid August (exact start/end dates can be negotiated between the student and MSPIRE faculty mentor). MSPIRE REUs spends part of the summer at the home institution of their MSPIRE faculty mentor and part of the summer at one of the Dutch facilities. See the MSPIRE Participant Locations Map on the Homepage for a complete listing of MSPIRE participating institutions.
Participants will receive a $5000 stipend and travel expenses (for travel to the Netherlands to carry out MSPIRE research). At some of the participating institutions, housing may also be provided,
The specific research project of each MSPIRE REU student and the research locations will strongly depend upon the identity and research interests of the MSPIRE faculty mentor. Participating MSPIRE faculty and their research interests are listed below.
MSPIRE Faculty and Their Research Interests
Mary T. Rodgers, Wayne State University
Chemistry, thermodynamics, and spectroscopy of protonated and metal-ligand complexes of analytical and biological relevance using tandem mass spectrometry techniques (ESI, FT-ICR MS, IRMPD) and electronic structure theory calculations. Applications to metal ion-amino acid complexes, metal ion-nucleobase complexes, tautomerization of protonated nucleobases and related heterocycles, metal ion-phosphate ester complexes, metal ion-nucleic acid complexes, and peptido-mimetic protonated base-crown ether complexes.
John R. Eyler, University of Florida
Use of tunable lasers to differentiate isomeric structures of carbohydrates and other biologically relevant species. Tunable CO2, optical parametric oscillator (OPO), and free electron lasers are used to produce infrared multiple photon dissociation (IRMPD) spectra and fragmentation patterns to distinguish between mono- and di-saccharide epimers and anomers, other isomeric intermediates in carbohydrate reactions (e.g., glycosyl oxocarbenium ions), and charged dimeric species of metabolic relevance (guanine, dopamine, cysteine, etc.)
Richard A. Yost, University of Florida
Fundamentals, instrumentation, and applications of mass spectrometry in analytical chemistry. Development of new mass spectrometric imaging and ion mobility instrumentation and techniques, and the application of these techniques in areas such as biomedical, pharmaceutical, environmental, petrochemical, and forensic chemistry.
I. Jonathan Amster, University of Georgia
The development of new FT-ICR techniques for the analysis of biological and synthetic macromolecules using laser desorption and electrospray ionization. Electron detachment dissociation and negative electron transfer dissociation for discerning the structural features of glycosaminoglycan oligosaccharides. Studies of FT-ICR fundamentals, including the effect of ion space-charge on the behavior of ions, using multiparticle computer simulations of ion motion.
Evan R. Williams, University of California, Berkeley
Our group is using the free electron laser to investigate how metal ions interact with the building blocks of life, focusing on amino acids and small peptides, to obtain a detailed understanding of the role of essential metal ions on peptide and protein structure and reactivity. State-of-the-art computational chemistry is used to model these interactions and as an aid to interpreting infrared spectra. These studies complement those done at Berkeley using an OPO laser to measure infrared spectra at higher frequencies to investigate competitive water binding interactions with metal ions and peptides. The ultimate goal of this research is to obtain a detailed understanding of how water and metal ions interact with and affect the structure and chemistry of proteins. Additional information about our research can be found at our group web site: (http://www.cchem.berkeley.edu/erwgrp/).
Peter B. Armentrout, University of Utah
Chemistry, thermodynamics, and spectroscopy of protonated and metal-ligand complexes of catalytic and biological relevance using tandem mass spectrometry techniques (ESI, FT-ICR MS, IRMPD) and electronic structure theory calculations. Applications to protonated and metal ion-amino acid complexes, metal crown ether complexes, and transition metal carbenes.
Brad K. Bendiak, University of Colorado-Denver
Structural differentiation of carbohydrate molecules using tandem mass spectrometry and variable wavelength photodissociation. Applications to monosaccharides, disaccharides, and product ion substructures of disaccharides with a goal of obtaining detailed structural information about the stereochemistry, anomeric configuration, and ring forms of key product ions derived from disaccharides and larger oligosaccharides via multi-stage tandem mass spectrometry. Isotopic labeling of carbohydrates performed in order to determine their precise origins.
Robert C. Dunbar, Case Western Reserve University
Spectroscopic analysis of conformations of metal-ion complexes with amino acids and small peptides, applying infrared IRMPD action spectroscopy with the free-electron laser. Conformational changes as a function of metal ion identity, peptide chain length, peptide sequence, side-chain interactions. Cation-pi interactions as a structure-determining feature involving aromatic residues. Computational vibrational spectroscopy complementary to the experimental observations. Metal-ion complexes with possible astrochemical relevance.
Nicholas C. Polfer, University of Florida
Our research focus is on reaction products from peptide fragmentation processes in mass spectrometry (MS). These products are structurally characterized by infrared photodissociation spectroscopy, in combination with harmonic frequency calculations at the density functional theory
(DFT) level. Our current emphasis is on peptide fragments from collision-induced dissociation (CID), but this will also be extended to reaction products from other dissociation techniques, such as electron transfer dissociation (ETD).
Please direct questions / send transcripts to:
Professor M. T. Rodgers
MSPIRE Summer REU Program
Wayne State University
5101 Cass Avenue, 33 Chemistry
Detroit, MI 48202