Bio

Rafael Brüschweiler received his Ph.D. in Physical Chemistry from ETH Zurich, Switzerland, before doing a postdoc at the Department of Molecular Biology at the Scripps Research Institute, La Jolla. 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 2013 with joint appointments at the Department of Chemistry and Biochemistry and the Department of Biological Chemistry and Pharmacology.  He is a full Professor, an Ohio Research Scholar (endowed), and the NMR Executive Director for the Ohio State Campus Chemical Instrument Center and the NSF-funded National Gateway Ultrahigh Field NMR Center to feature the first 1.2 GHz NMR Spectrometer in the U.S. His research is funded primarily by the National Science Foundation and the National Institutes of Health. 

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 interactions of proteins 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 to enhance resolution, sensitivity, and speed. Biological systems studied in the lab include the following proteins: the GTPase K-Ras and its oncogenic mutants, p53/MDM2, sodium-calcium exchanger NCX, Cu2+-ATPase, ubiquitin, and the enzymes arginine kinase and glucokinase. Metabolic studies are conducted on opportunistic biofilm-forming microbes, such as Pseudomonas aeruginosa and Staphylocuccus aureus, drosophila, E. coli, yeast, and cancer cell lines for the identification of biomarkers, biochemical pathways and the characterization of novel metabolites in health and disease. We also combine biophysical chemistry with nano-science, for example, for nanoparticle-assisted NMR spin relaxation. We also develop machine-learning tools for the better and automated analysis and interpretation of NMR data. 

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) toward a predictive understanding of complex biomolecular systems, (3) complex mixture analysis and metabolomics by NMR for biomedical diagnostics in collaboration with the OSU Medical School, and/or (4) the development of new NMR methods (pulse sequences, enhanced sampling, rapid spectral reconstruction). Graduate students from any of the chemistry (bio, physical, analytical) programs, the Biophysics program, and OSBP are encouraged to contact Dr. Brüschweiler to learn more about his group's research, meet current graduate students and postdocs in the lab, and discuss the possibility of a research rotation. More detailed information can be found on the Brüschweiler website.

Past members of the Brüschweiler group have been successful in a wide range of professional positions in the US and abroad in industry, national labs, and academia. 

Publications

For a full list of publications, click here.

Yuan, C., Hansen, A.L., Bruschweiler-Li, L. and Bruschweiler, R; NMR ¹H, ¹³C, ¹⁵N backbone resonance assignments of wild-type human K-Ras and its oncogenic mutants G12D and G12C bound to GTP. Biomol NMR Assign 18, 7–13 (2024).

Hansen, A.L., Xiang, X., Yuan, C., Bruschweiler-Li, L. and Bruschweiler, R; Excited-state observation of active K-Ras reveals differential structural dynamics of wild-type versus oncogenic G12D and G12C mutants. Nat Struct Mol Biol 30, 1446–1455 (2023).

Ma P, Li D-W, Brüschweiler R. Predicting protein flexibility with AlphaFold. Proteins. 2023; 91(6): 847–855.

Li, D.-W., Bruschweiler-Li, L., Hansen, A. L., and Brüschweiler, R.; DEEP Picker1D and Voigt Fitter1D: a versatile tool set for the automated quantitative spectral deconvolution of complex 1D-NMR spectra, Magn. Reson., 4, 19–26.

Allpas, R. C., L. Hansen, A., & Rafael Brüschweiler; Arche-Noah: NMR supersequence with five different CEST experiments for studying protein conformational dynamics. Physical Chemistry Chemical Physics. 2023, 25, 16217-16221