rienstra group home people research publications news links funding contact

dr. Kathryn D. Kloepper

Kathryn Kloepper

ph.d., analytical chemistry (2003-2008)

  • Assistant Professor of Physical Chemsitry at St Lawrence University in Canton, NY
  • Ph.D. UIUC, Analytical Chemistry in 2008
  • B.S. in Chemistry from the University of Dallas in 2003
  • I am originally from Auburn, AL and obtained my B.S. in chemistry from the University of Dallas in May 2003 and joined the Rienstra group that November. In the Rienstra group I studied alpha-synuclein, a 140-residue protein of unknown function that is the primary component of Lewy bodies, the pathological hallmark of Parkinson's disease. Wild-type (WT) and the PD-associated mutants (A53T, A30P, E46K) aggregate into fibrils in vitro. Little is known about the mechanism or structure of alpha-synuclein fibrils, despite its implication in this disease. During my first year in the Rienstra group, I optimized the expression and purification of isotopically labeled alpha-synuclein in order to study the structure of alpha-synuclein fibrils by SSNMR (Kloepper, et al., 2006). I also studied several states of alpha-synuclein by SSNMR, mass spectrometry and fluorescence spectroscopy. This work was performed in collaboration with the laboratory of Prof. Julia M. George.

    An atomic-resolution structure of alpha-synuclein fibrils may help elucidate the role of the protein in Parkinson’s disease. Reproducible fibril samples of wild-type and the three disease-relevant mutants have been prepared with both uniform and selective isotopic labeling schemes, permitting a comparison of secondary structure and dynamics wild-type and the early-onset mutants A53T and A30P. Low temperature data acquisition results in improved spectral sensitivity, permitting acquisition of three- and four-dimensional spectra. The majority of the fibril core resonances have been assigned. Recently, investigation of the effects of hydration on fibril structure demonstrates that water is nonessential to the fibril core structure.

    I am a member of the American Chemical Society and the University of Illinois Women Chemists Committee. I have also volunteered as a first-year mentor and a high school Science Olympiad judge at regional, state, and national competitions.

    I have also supervised several undergraduate researchers including Kem Winter, Dan Graesser, Brian Money, Daniel Ladror, Kevin Hartman, and Reika Ebisu in developing high-yield expresson and purification protocols for natively unfolded proteins such as alpha-synuclein.

    Currently, I am working as a Visiting Assistant Professor of Physical Chemistry at St Lawrence University in Canton, NY.

  • Curriculum Vitae
  • Honors and Awards

  • John R. Beck Fellowship, 2006-2007
  • Departmental Fellowship, 2005-2006
  • publications (with rienstra group)(pubmed)

    (6) “Solid-state NMR spectroscopy reveals that water is nonessential to the core structure of alpha-synuclein fibrils”, Kloepper, K. D.; Hartman, K. L.; Ladror, D. T.; Rienstra, C. M. J. Phys. Chem. B 2007, 111, 13353-13356. (Published online, November 7, 2007).

    (5) “Conformation-specific binding of alpha-synuclein to novel protein partners detected by phage display and NMR spectroscopy”, Woods, W. S.; Boettcher, J. M.; Zhou, D. H.; Kloepper, K. D.; Hartman, K. L.; Ladror, D. T.; Qi, Z.; Rienstra, C. M.; George, J. M. J. Biol. Chem. 2007, 282, 34555-34567. (Published online, September 24, 2007.).

    (4) “Temperature-dependent sensitivity enhancement of solid-state NMR spectra of alpha-synuclein fibrils”, Kloepper, K. D.; Zhou, D. H.; Li, Y.; Winter, K. A.; George, J. M.; Rienstra, C. M., J. Biomol. NMR 2007, 39, 197-211. (Published online September 28, 2007).

    (3) “Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins”, Franks, W. T.; Kloepper, K. D.; Wylie, B. J.; Rienstra, C. M., J. Biomol. NMR 2007, 39, 107-131. (Published online August 9, 2007)

    (2) “Band-selective 13C homonuclear 3D spectroscopy for solid proteins at high field with rotor-synchronized soft pulses”, Zhou, D. H.; Kloepper, K. D.; Winter, K. A.; Rienstra, C. M., J. Biomol. NMR 2006, 34, 245-257. (Published online, February 10, 2006).

    (1) “Preparation of alpha-synuclein fibrils for solid-state NMR: Expression, purification and incubation of wild type and mutant forms”, Kloepper, K. D.; Woods, W. S.; Winter, K. A.; George, J. M.; Rienstra, C. M., Protein Expr. Purif. 2006, 48, 112-117. (Published online, March 10, 2006 ).