Markus Voehler
Research Associate Faculty
Director of Operation Biomolecular NMR
Dr. Voehler is not currently accepting graduate students.
I have the pleasure to direct the Biomolecular NMR Facility of the Vanderbilt Center for Structural Biology as well as interact with the Small Molecular NMR facility. We have nine state-of- the-art NMR instruments total ranging from 400 to 900 MHz enabaling experiments for a variety of research. We also provide graduate, postdoctoral students, or faculty with the necessary expertise to help in the experiment selection and execution through formal NMR workshops or one on one training at various levels. There are formal classes (Chem 3320, BioChem 8343) that cover NMR theory and interpretation of NMR spectra. Our main research in the Biomolecular NMR Facility focusses on protein and DNA biomolecules, where we study complex biomolecular assemblies, membrane proteins, molecular dynamics conformational exchange processes, or ligand binding interactions, including fragment-based NMR screens for drug discovery. Work with these larger systems has been facilitated by the advent of TROSY based measurements, at magnetic field strengths of 800 MHz or greater. Work in the Small Molecule Facility evolves around compound verification and structural elucidation of small molecules from organic synthesis, natural compounds, organo-metallics, polymers, and many more. NMR based matabolomic- and lipodomic profiles can be measured with our In-Vitro-Diagnostic research equipment (IVDr) on biofluids like urine, plasma, serum or cerebrospinal fluid (CSF). |
Specializations
Biophysical Chemistry |
Representative Publications
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1. Castro, M. A.; Parson, K. F.; Beg, I.; Wilkinson, M. C.; Nurmakova, K.; Levesque, I.; Voehler, M. W.; Wolfe, M. S.; Ruotolo, B. T.; Sanders, C. R., Verteporfin is a Substrate-Selective gamma-Secretase Inhibitor that Binds the Amyloid Precursor Protein Transmembrane Domain. J Biol Chem 2022, 101792 2. Voehler, M.; Ashoka, M. A.; Meiler, J.; Bock, P. E., Carbon and amide detect backbone assignment methods of a novel repeat protein from the staphylocoagulase in S-aureus. Biomolecular NMR Assignments 2017, 11 (2), 243-249. 3. Voehler, M. W.; Eoff, R. L.; McDonald, W. H.; Guengerich, F. P.; Stone, M. P., Modulation of the Structure, Catalytic Activity, and Fidelity of African Swine Fever Virus DNA Polymerase X by a Reversible Disulfide Switch. Journal of Biological Chemistry 2009, 284 (27), 18434-18444. 4. Vanacore, R.; Ham, A. J. L.; Voehler, M.; Sanders, C. R.; Conrads, T. P.; Veenstra, T. D.; Sharpless, K. B.; Dawson, P. E.; Hudson, B. G., A Sulfilimine Bond Identified in Collagen IV. Science 2009, 325 (5945), 1230-1234. 5. Voehler, M. W.; Collier, G.; Young, J. K.; Stone, M. P.; Germann, M. W., Performance of cryogenic probes as a function of ionic strength and sample tube geometry. J Magn Reson 2006, 183 (1), 102-109. |