Research
    The Biomolecular NMR Core Facility provides support across the Biological Sciences Division at the University of Chicago. A partial list of the research currently actively supported by the facility includes

    • The Meredith group, who examines the root causes of Alzheimer’s disease, which is caused by the misfolding of a protein in the brain.
      • website link http://bmb.uchospitals.edu/faculty/stephen-meredith
      • Adam L. Cloe, Joseph P. R. O. Orgel, Joseph R. Sachleben, Robert Tycko, Stephen C. Meredith. “The Japanese Mutant Aβ (ΔE22-Aβ1–39) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence Seeding of Wild-Type Aβ1–40 into Atypical Fibrils by ΔE22-Aβ1–39.” Biochemistry. 50 (2011) 2026-2039. 2011-DelE22Abeta
    • The Sosnick group, who examines protein folding.
      • website link  http://sosnick.uchicago.edu/
      • Skinner, J. J., Yu, W., Gichana, E. K., Baxa, M. C., Hinshaw, J. R., Freed, K. F., and Sosnick, T. R. (2014) Benchmarking all-atom simulations using hydrogen exchange, Proc Natl Acad Sci U S A. PNAS-2014-Skinner
      • Zayner, J. P., and Sosnick, T. R. (2014) Factors that control the chemistry of the LOV domain photocycle, PLoS One 9, e87074. 3903614 PLOS1-2014-Zayner
      • Zayner, J. P., Antoniou, C., French, A. R., Hause, R. J., Jr., and Sosnick, T. R. (2013) Investigating models of protein function and allostery with a widespread mutational analysis of a light-activated protein, Biophys J 105, 1027-1036. 3752136 BiophysJ-2013-Zayner
    • The Perozo group, who study ion channels, which are crucial for nerve conduction.
      • website link  http://bmb.bsd.uchicago.edu/faculty/eduardo-perozo
      • Raymond E. Hulse, Joseph R. Sachleben, Po-Chao Wen, Mahmoud Moradi, Emad Tajkhorshid, Eduardo Perozo. “Conformational Dynamics at the Inner Gate of KcsA During Activation.” Biochemistry. 53 (2014) 2557-59. DOI: 10.1021/bi500168u. 2014-KcsA
    • The Turner laboratory, which investigates the role of the proteins that seal the cells of the intestinal lining together in inflammatory bowl disease (IBD).
    • The Macleod and Conzen laboratories, who utilize the facility to perform metabolic analysis of cancerous cells.
    • The Adams group examines the protein interactions responsible for immune response.
    • The Thornton group is looking at the evolution of protein function.
    • The Pan group is has probed the structure changes in RNA caused by methylation

     

    We also actively develop new methods to assist our users in approaching their scientific problems.

     

    ALCHIM

    Aliphatic Chain Length by Isotropic Mixing (ALCHIM) is a 1H NMR technique for identifying saturated and unsaturated acyl groups in complex mixtures of lipids by using a selective TOCSY technique. It can distinguish ω-3, ω-6, and ω-9 unsaturated fatty acid and has shown to be effective in samples relevant to food science (coconut oil) and biomedical sciences (neutral fats extracted from mouse adipose tissue). We also demonstrate that it can be used in whole adipocytes indicating that it will have applications in whole tissues. This technique provides researchers to a new tool for probing lipid samples in biomedically relevant samples.

    Paper: Joseph R. Sachleben, Ruiyang Yi, Paul Volden, Suzanne Conzen. “Determining Fatty Acid Compositon of Metabolomic Samples by 1H NMR Spectroscopy.” J. Biomol. NMR. 59 (2014) 161-173. DOI: 10.1007/s10858-014-9836-0. 2014-ALCHIM
    Supplemental Information: 2014-ALCHIM-OR1 & 2014-ALCHIM -OR2
    Mathematica notebook for fitting ALCHIM curves: ALCHIM_binmixfit.nb