Thomas Szyperski


Thomas Szyperski.

Thomas Szyperski


Thomas Szyperski


Research Interests

Nuclear magnetic resonance (NMR)-based structural biology, structural genomics and metabonomics: NMR methodology development, applications to study protein structure, dynamics and folding, metabolic profiling.

Contact Information

816 Natural Sciences Complex

Buffalo NY, 14260

Phone: (716) 645-4309

Fax: (716) 645-6963


  • Fellow im Verband der Chemischen Industrie, 1989-1991
  • Fellow of the Studienstiftung des Deutschen Volkes, 1982-1988
  • Visiting scientist, U Auckland (NZ), 1988
  • Habilitation, ETH Zürich (CH), 1998
  • Dr. sc. nat ETH, ETH Zürich (CH), 1992
  • Diploma Chemistry, TU Munich (D), 1988
  • Prediploma Chemistry, TU Munich (D), 1985
  • Prediploma Biochemistry, U Tübingen (D), 1984

Awards and Honors


Structure determination of biological macromolecules using nuclear magnetic resonance (NMR) spectroscopy, Development of Bio-NMR techniques, Structural genomics, Metabonomics.

Research Summary

Our research focuses on:

  • Development of Bio-NMR methodology.
  • Structure determinations of biological macromolecules using nuclear magnetic resonance (NMR) spectroscopy.
  • Development of NMR-based structural biology in supercooled water.
  • Investigation of cellular metabolism in support of biotechnology research.
  • Metabonomics

Selected Recent Publications

  • Sathyamoorthy, B., Parish, D.M., Montelione, G.T., Xiao, R., Szyperski, T. (2014) Spatially Selective Heteronuclear Multiple-quantum (HMQC) Spectroscopy for Bio-molecular Studies. ChemPhysChem 15:1872-1879. PMID:24789578.
  • Liu, G., Poppe, L., Aoki, K., Yamane, H., Lewis, J., Szyperski, T. (2014) High-quality NMR Structure of Human Anti-apoptotic Protein Domain Mcl-1(171-327) for Cancer Drug Design.
    PLoS One 9:e96521. PMID:24789074
  • Pulavarti, S.V., Eletsky, A., Huang, Y.J., Acton, T.B., Xiao, R., Everett, J.K., Montelione, G.T., Szyperski, T. (2015) Polypeptide Backbone, Cb and Methyl Group Resonance Assignments of the 24 kDa Plectin Repeat Domain 6 from Human Protein Plectin. J. Biomol. NMR Assign. 9:135-138. PMID: 24722902
  • Wu, X., Liu, R., Sathyamoorthy, B., Yamato, K., Liang, G., Shen, L., Ma, S., Sukumaran, D.K., Szyperski, T., Fang, W., He, L., Chen, X., Gong, B. (2015) Discrete Stacking of Aromatic Oligoamide Macrocycles. J. Am. Chem. Soc. 137:5879-5882. PMID:25909625
  • Eletsky, A., Pulavarti, S.V., Beaumont, V., Gollnick, P., Szyperski, T. (2015) Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes. J. Am. Chem. Soc. 137:11242-11245. PMID:26293598
  • Bhardwaj, G., Mulligan, V. K., Bahl, C. D., Gilmore, J. M., Harvey, P. J., Cheneval, O., Buchko, G. W., Pulavarti, S. V., Kaas, Q., Eletsky, A., Huang, P. S., Johnson, W. A., Greisen, P. J., Rocklin, G. J., Song, Y., Linsky, T. W., Watkins, A., Rettie, S. A., Xu, X., Carter, L. P., Bonneau, R., Olson, J. M., Coutsias, E., Correnti, C. E., Szyperski, T., Craik, D. J., Baker, D. (2016) Accurate de Novo Design of Hyperstable Constrained Peptides. Nature 538: 329-335. PMID:27626386
  • Jacobs, T. M., Williams, B., Williams, T., Xu, X., Eletsky, A., Federizon, J. F., Szyperski, T., Kuhlman, B. (2016) Design of Structurally Distinct Proteins Using Strategies Inspired by Evolution. Science 352: 687-690. PMID: 27151863
  • Szyperski, T. (2017) Preview: Room Temperature X-Ray Crystallography Reveals Conformational Heterogeneity of Engineered Proteins. Structure 25: 691-692. PMID:28467914
  • Zhang, M., Yu, X.W., Xu, Y., Jouhten, P., Swapna, G.V.T., Glaser, R.W., Hunt, J.F., Montelione, G.T., Maaheimo, H., Szyperski T. (2017) 13C Metabolic Flux Profiling of Pichia pastoris Grown in Aerobic Batch Cultures on Glucose Revealed High Relative Anabolic Use of TCA Cycle and Limited Incorporation of Provided Precursors of Branched-chain Amino Acids. FEBS J: 284: 3100-3113. PMID:28731268
  • Rosarion-Cruz, Z., Eletsky, A., Daigham, N.S., Al-Tameemi, H., Swapna, G.V.T., Kahn, P.C., Szyperski, T., Montelione, G.T., Boyd, J.M. (2019) The copBL Operon Protects Staphylococcus aureus from copper toxicity: CopL is an Extracellular Membrane-associated Copper-binding Protein. J. Biol. Chem. 294: 4027-4044. PMID: 30655293