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    Eric Oldfield, PhD

    A110 Chemical & Life Sciences Laboratory
    600 South Mathews Ave.
    Urbana IL, 61801
    Phone: (217) 333-3374
    Fax: (217) 244-0997


    Professor of Chemistry and Biophysics
    Phone: (217) 333-3374
    FAX: (217) 244-0997

    Bristol University, England, BSc 1966-1969; DSc, 1982, Chemistry
    Sheffield University, England, PhD, 1969-1972, Biophysical Chemistry
    Indiana University, Bloomington, Indiana, Postdoctoral, 1972-1974, Biophysical Chemistry
    M.I.T., Cambridge, Massachusetts, Postdoctoral, 1974-1975, Chemistry

    Awards and Fellowships:
    Thomas Malkin Prize (1968)
    William Edward Garner Prize (1969)
    European Molecular Biology Organization Fellowship (1972-1974)
    The Meldola Medal and Prize of The Royal Institute of Chemistry (1977)
    Alfred P. Sloan Research Fellowship (1978-1980)
    U.S. Public Health Service Research Career Development Award (1979-1984)
    American Heart Association Louis N. Katz Basic Science Research Prize (1980)
    Fellow of the Royal Society of Chemistry (1981)
    Fellow, American Institute of Chemists (1982)
    The Colworth Medal of the Biochemical Society (1983)
    American Chemical Society Award in Pure Chemistry (1984)
    Fellow, American Physical Society (1993)
    Richard G. and Carole J. Cline University Senior Scholar (1995)
    Royal Society of Chemistry Award in Spectroscopy (1995)
    Associate, Center for Advanced Study (2000-2001)
    Alumni Research Scholar Professor of Chemistry (2003-2013)
    Campus Award for Excellence in Guiding Undergraduate Research (2006)
    Fellow, American Association for the Advancement of Science (2008)
    Royal Society of Chemistry Award in Soft Matter and Biophysical Chemistry (2010)
    Biophysical Society Avanti Award in Lipids (2011)
    Harriet A. Harlin Professor of Chemistry (2012)

    Positions Held:
    ILEA Undergraduate, Bristol University, 9/66-6/69, with Professor Jake MacMillan, FRS, Professor Geoffrey Eglinton, FRS.
    SRC Scholar, Sheffield University, 10/69-5/72, with Professor Dennis Chapman, FRS
    EMBO Fellow and Research Associate, Indiana University, 7/72-12/74, with Professor Adam Allerhand
    Visiting Scientist, Massachusetts Institute of Technology, 1/75-6/75, with Professor John S. Waugh
    Assistant Professor of Chemistry, University of Illinois at Urbana-Champaign, 1975-1980
    Fellow, Center for Advanced Study, 1979-1980
    Associate Professor of Chemistry, University of Illinois at Urbana-Champaign, 1980-1982
    Professor of Chemistry, University of Illinois at Urbana-Champaign, 1982-2003
    Professor of Biophysics, 1995-present date
    Alumni Research Scholar Professor of Chemistry, 2003-2012
    Harriet A. Harlin Professor of Chemistry, 2012-present

    Chemistry 109 Freshman Chemistry
    Chemistry 110 Freshman Chemistry
    Chemistry 340 Introductory Physical Chemistry
    Chemistry 344 Kinetics, Thermodynamics, Statistical Mechanics
    Chemistry 348 Advanced Physical Chemistry
    Chemistry 383 Dynamics, Structure and Physical Methods
    Chemistry 385 Chemical Fundamentals
    Chemistry 440 Biophysical Chemistry
    Chemistry 449 Special Topics: Heteronuclear NMR
    Chemistry 450 Student Seminar

    Committees, etc.:
    JACS, Editorial Advisory Board
    Antimicrobial Agents and Chemotherapy, Editorial Advisory Board
    Faculty Senator, University of Illinois at Urbana-Champaign Senate
    Search Committee for Head, Department of Chemistry
    Chair, American Chemical Society-Biophysical Chemistry Sub-Division
    Editorial Board, Spectroscopy
    Editorial Board, Journal of Magnetic Resonance
    Advisory Committee, NSF National High Magnetic Field Laboratory
    Editorial Advisory Board, Magnetic Resonance Reviews
    Editorial Board, Solid State NMR
    Editorial Board, Chemistry and Physics of Lipids
    Editorial Advisory Board, The Biochemical Journal
    Chair, School of Chemical Sciences Awards Committee
    Search Committee for Director, School of Chemical Sciences
    Department of Chemistry General Chemistry Committee
    IBM-University Shared Instrumentation Review Committee
    Continuing Graduate Student Committee
    Chemical and Life Sciences Building Committee
    Staff Committee
    Graduate Fellowships Committee
    Physical Chemistry Graduate Student Recruiting Committee
    Biophysical Chemistry Advising
    Safety Committee
    Service Facilities Committee
    Pre-Med Students Committee
    Executive Committee, Experimental NMR Conference, Inc.

    Mobil Research and Development Corporation
    Shell Oil Company
    Allied-Signal (UOP)
    Engelhard Corporation
    Spectral Data Services, Incorporated
    Morgan and Finnegan, New York (in re Mobil v. Amoco)
    Arnold, White and Durkee, Houston (in re Shell v. Union Carbide)
    Lockwood, Alex, Fitzgibbon and Cummings, Chicago (in re Morton Thiokol v. Argus Witco)

    Society Memberships:
    The Biophysical Society
    The Royal Society of Chemistry
    The American Physical Society
    The American Chemical Society
    The American Institute of Chemists
    The Biochemical Society (London)
    The American Heart Association (Council on Basic Science)
    American Association for the Advancement of Science
    American Society for Microbiology

    Research background and Interests

    I was educated in London, Bristol and Sheffield, then moved to the US as a European Molecular Biology Organization Fellow at Indiana University with Adam Allerhand and a Visiting Scientist at MIT with John Waugh. I am currently a Professor of Chemistry and a Professor of Biophysics. At Sheffield, we developed the deuterium NMR method to investigate the structures of liquid crystals and biological membranes. We synthesized specifically 2H-labeled phospholipids and were able to show that 2H NMR quadrupole splittings were an important new probe of lipid bilayer structure, and that sterols such as cholesterol caused large increases in hydrocarbon chain order parameters. At Illinois, we then showed that specific 2H-labeling of lipid headgroups enabled a detailed picture of headgroup conformation to be obtained, and the general success of the deuterium NMR method for investigating liquid crystal and membrane structure can be seen from its use by many groups worldwide, where order parameters from 2H spectra give the most detailed view of membrane order and dynamics available so far. Together with A. Allerhand, we developed novel, high sensitivity Fourier transfer NMR instrumentation and observed the first carbon-13 NMR spectra of proteins, which began to open up new areas of research by demonstrating that carbon-13 spectra of proteins could be extremely highly resolved, and carbon-13 NMR of proteins in solution is now considered a routine technique to obtain static and dynamic information about the structure of macromolecules in solution.

    We then began to develop new ways of obtaining high resolution solid state NMR spectra of inorganic and biological systems. We showed that high-resolution NMR spectra of quadrupolar nuclei in inorganic solids could often be obtained by observing the so-called central (1/2 -1/2) transition, which is only broadened to second-order by the quadrupole interaction. At high magnetic fields, the effect is small, and we demonstrated that it could be further reduced by spinning at unusual angles in the magnetic field - the variable-angle sample spinning approach. We then pursued the use of oxygen-17 NMR in investigating inorganic solids such as silicates and zeolites, where we found that accurate chemical shifts, quadrupole coupling constants and asymmetry parameters could all be obtained, and interpreted in detailed structural terms. This work was then extended into the realm of solid-state physics via investigations of relaxation processes in oxides and high-temperature superconductors, then into the biological area via studies of oxygen-17 labelled oxygen and carbon monoxide bonding to proteins, such as hemoglobin.

    We also showed that exceptionally well resolved carbon and proton spectra of lipid bilayers could be obtained, by using high field "magic-angle" sample spinning techniques. Our results provided greatly enhanced resolution over obtained using sonicated bilayers, due in large part to the inhomogeneous nature of the dipolar interactions, and the lack of linebroadening due to vesicle tumbling, opening up new ways to investigate membrane structure.

    We subsequently began to work on solving the chemical shift problem in proteins, identified earlier - how does folding a protein into its native conformation generate very large chemical shift nonequivalencies? In the early 1990's, we began to use ab initio and density functional quantum chemical methods (typically used by theorists to study much smaller molecules) to try to compute the chemical shifts of carbon-13 and nitrogen-15 nuclei in proteins. It worked, and we demonstrated that it is possible to accurately predict chemical shifts of C-13, N-15 and F-19 nuclei in proteins, work that is adding a "new dimension" to protein structure studies, as well as solving a long-standing spectroscopic problem. Moreover, our most recent results show that accurate backbone and sidechain structural (torsion angle) parameters can be obtained from chemical shifts, and that protein structures can begin to be refined by using such chemical shift information.

    This work was then extended to investigating metal-ligand bonding in heme proteins, where we combined solid state NMR, solution NMR, Mössbauer and infrared spectroscopy and quantum chemistry to investigate in detail how small molecules, such as oxygen and carbon monoxide, bind to heme proteins, such as hemoglobin and myoglobin. The problem of how CO and oxygen are discriminated in their binding has been a topic of lively debate for over 20 years, with early crystallographic studies indicating CO binds in a "bent" manner, which is destabilizing, this being the textbook model of CO/oxygen discrimination. However, by using density functional theory to analyze C-13, O-17 and Fe-57 NMR chemical shifts, 57Fe Mössbauer quadrupole splittings and infra-red spectroscopic results, we were able to demonstrate that CO binds in a close-to-linear and untilted fashion to hemoglobin and myoglobin. This strongly supports the idea that it is the stabilization of oxygen binding (via hydrogen bonding) rather than CO-destabilization, which is the origin of CO/oxygen discrimination.

    In addition to these studies of metal-CO interactions in biological systems, we have also made extensive investigations in collaboration with A. Wieckowski, into the topic of how CO binds to metals in heterogeneous catalysts, in particular those used in fuel cells. We have shown that by using high field NMR it is possible to readily investigate both the metal sites (via Pt-195 NMR) and the ligands (via C-13 NMR), and that there is a clear relationship between the Knight shift of the CO molecules bound to the catalyst surfaces and the electronic local density of states at the Fermi level of the Pt catalysts, which opens up exciting new possibilities of using NMR to probe the electronic properties of many other heterogeneous catalysts.

    In recent work, carried out in collaboration with the groups of J. Urbina, R. Docampo and S. Croft, we have branched out into yet another new area, molecular parasitology. We first found evidence for extremely large levels of inorganic di- and triphosphate in the protozoa which cause African sleeping sickness and malaria. This then led us to the idea that it might be possible to kill these and other related parasites by using stable diphosphate analog drugs to block specific metabolic pathways, and this indeed was found to be the case. The drugs used, called bisphosphonates, have been used to treat bone-resorption diseases for over 20 years, but their mode of action had been unknown. However, in recent work, we have shown that the most potent, nitrogen-containing bisphosphonates used in treating bone diseases are also potent drugs in killing parasites, and act to perturb protein prenylation and signaling by inhibiting the enzyme farnesyl pyrophosphate synthase. Using quantum chemistry and molecular modeling, we showed that the charged ammonium side-chains in the drugs act as carbocation transition state analogs, and bind into the active site of the enzyme, blocking its action. This gives a sound molecular basis for drug design, based on known protein structures and mechanisms of drug action, and is a topic of considerable current interest.

    And finally, in our most recent work we have found that it is possible to apply the computational methods used in modern drug design and drug discovery to the immune system where we are employing QSAR (quantitative structure activity relationships) to probe innate immunity. In particular, we are interested in the development of drugs which activate γδ T cells, opening the way to new therapies for infectious diseases, cancer, and vaccine development.

    (c) 2010-2015 Research Group of Professor Eric Oldfield
    University of Illinois at Urbana-Champaign

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