Rafael Brüschweiler

Rafael Brüschweiler

Rafael Brüschweiler

Ohio Research Scholar



382 CBEC Building
151 W Woodruff Ave
Columbus, OH 43210

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Areas of Expertise

  • Biochemistry
  • Physical


Rafael Brüschweiler received his Ph.D. in 1991 in Physical Chemistry from ETH Zurich, Switzerland, before doing a postdoc at the Department of Molecular Biology at the Scripps Research Institute, La Jolla. In 2004, he joined the Florida State University, Tallahassee, as full professor and the National High Magnetic Field Laboratory as Associate Director for Biophysics.  Professor Brüschweiler joined Ohio State in August 2013 with joint appointments at the Department of Chemistry and Biochemistry and at the College of Medicine.  He is an Ohio Reseach Scholar.  He is also NMR Executive Director for the Ohio State Campus Chemical Instrument Center.

Research Overview

Professor Brüschweiler's research is highly cross-disciplinary in the area of biophysical chemistry as well as analytical chemistry. It focuses on the understanding of the role of dynamics and thermodynamics of proteins properties for their function and on the analysis of complex biological mixtures in the context of metabolomics. The main research tools are high-field nuclear magnetic resonance (NMR) and high-performance computation, which includes the development of new and improved techniques. Biological systems studied in the lab include the proteins p53/MDM2, sodium-calcium exchanger NCX, Cu2+-ATPase, ubiquitin, and the enzymes arginine kinase and glucokinase. Metabolic studies are conducted on drosophila, E. coli, yeast, and cancer cell lines in combination with isotope labeling, such as carbon-13.

Dr. Brüschweiler is accepting new graduate students for the Fall that have interest in studying (1) protein dynamics, interactions, and function by state-of-the-art NMR spectroscopy, (2) protein dynamics and function by computational methods (molecular dynamics simulations) in combination with experimental data, (3) complex mixture analysis and metabolomics by NMR, computation, and other methods, and/or (4) development of new NMR methods (pulse sequences, sparse sampling, covariance spectroscopy). Graduate students from any of the chemistry (physical, bio, analytical) and chemical physics programs are encouraged to request a meeting to discuss possible projects. More detailed research information can be found on the Brüschweiler website.

Recent members of the Brüschweiler group now hold faculty positions at the University of Sao Paulo, the Technical University Eindhoven, Penn State, William Patterson University, Western Washington University, College of Mount St. Joe, Peking University, and Fudan University.


Li, D.-W.; Showalter, S.A.; Brüschweiler, R. J. Phys. Chem. B 2010,114: 16036-16044. Entropy localization in proteins.

Li, D-W.; Brüschweiler, R. J. Chem. Theor. Comput. 2011, 7: 1773-1782. Iterative optimization of molecular mechanics force fields from NMR data of full-length proteins.

Niu, X.; Bruschweiler-Li, L.; Davulcu, O.; Skalicki, J.; Brüschweiler, R.; Chapman, M.S. J. Mol. Biol 2011, 405: 479-496. Arginine kinase: Joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility.

Long, D.; Brüschweiler, R. PLoS Comput. Biol. 2011, 7: e1002035. In silico elucidation of the recognition dynamics of ubiquitin.

Salinas, R.K.; Bruschweiler-Li, L.; Johnson, E.; Brüschweiler, R. J. Biol. Chem. 2011, 286: 32123 – 32131. Ca2+ binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the Na+/Ca2+ exchanger.

Long, D.; Li, D.-W.; Walter, K. F.; Griesinger, C.; Brüschweiler, R. Biophys. J. 2011, 101: 910-915. Toward a predictive understanding of slow methyl group dynamics in proteins.

Bingol, K.; Brüschweiler, R., Anal. Chem. 2011, 3, 7412-7417. Deconvolution of Chemical Mixtures with High Complexity by NMR Consensus Trace Clustering.

Long, D.; Brüschweiler, R. J. Am. Chem. Soc. 2011, 133: 18999-19005. Atomistic kinetic model for population shift and allostery in biomolecules.

Shan, B.; Li, D.-W.; Bruschweiler-Li, L.; Brüschweiler, R. J. Chem. Biol. 2012, 287: 30376-30384. Competitive binding between dynamic p53 transactivation subdomains to human MDM2: Implications for regulating the p53:MDM2/MDMX interaction.

Long, D; Brüschweiler, R. J. Phys. Chem. Letters 2012, 3: 1722-1726. Structural and entropic allosteric signal transduction strength via correlated motions.

Li, D-W.; Brüschweiler, R. J. Chem. Theor. Comput. 2012, 8: 2531-2539. Dynamic and thermodynamic signatures of native and non-native protein states with application to the improvement of protein structures.

D.-W. Li and R. Brüschweiler, J Biomol NMR. 2012, 3: 257-265. PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles.

Larion, M.; Salinas, R.K.; Bruschweiler-Li, L; Miller, B.; Brüschweiler, R. PLoS Biology 2012, 10: e1001452. Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinase.

Anderson, K.M.; Esadze, A.; Manoharan, M.; Brüschweiler, R.; Gorenstein, D.G.; Iwahara, J. J. Am. Chem. Soc. 2013, 135: 3613-3619. Direct observation of the ion-pair dynamics at a protein-DNA interface by NMR spectroscopy.

Long, D.; Brüschweiler, R. Angew. Chem. 2013, 52: 3709-3711. Directional selection precedes conformational selection in ubiquitin-UIM binding.

Li, D.-W.; Brüschweiler, R. J. Chem. Theory Comput. 2014, 10: 1781–1787. Protocol To Make Protein NMR Structures Amenable to Stable Long Time Scale Molecular Dynamics Simulations.

Bingol, K.; Zhang, F.; Bruschweiler-Li, L.; Brüschweiler, R. J. Am. Chem. Soc. 2012, 21: 9006-9011. Carbon Backbone Topology of the Metabolome of a Cell.

Bingol, K.; Zhang, F.; Bruschweiler-Li, L.; Brüschweiler, R., Anal. Chem. 2012, 84: 9395-9401.TOCCATA, A Customized Carbon Total Correlation Spectroscopy NMR Metabolomics Database.

Bingol, K.; Zhang, F.; Bruschweiler-Li, L.; Brüschweiler, R., Anal. Chem. 2013, 85: 6414-6420. Quantitative analysis of metabolic mixtures by 2D 13C constant-time TOCSY NMR spectroscopy.

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