个人简介
Beat H. Meier is a full Professor of physical chemistry at ETH Zurich since July 1998. His research group works in the field of solid-state NMR spectroscopy.
Beat Meier was born in 1954 in Solothurn (Switzerland). He received his Diploma in Chemistry in 1978 and his Ph. D. (under supervision of R.R. Ernst) in 1984, both from ETH Zurich. After two years as a postdoc at the Los Alamos National Labs (USA), he returned to ETH as a staff scientist where he habilitated in 1993. In 1994 he moved to the University of Nijmegen as a full professor in Physical Chemistry and member of the board of the National High-Field NMR facility and the NSR research center.
研究领域
Solid-state NMR Spectroscopy
Research interests include the development of new methods and the improvement on existing pulse sequences in solid-state NMR, with particular emphasis on polarization-transfer techniques, the refinement of the theoretical concepts for the description of spin systems under time-dependent Hamiltonians as well as numerical simulations and the study of local ordering phenomena in macroscopically disordered systems, e.g. glasses, amorphous synthetic polymers, biopolymers and polymerblends using NMR techniques.
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A. K. Schütz, T. Vagt, M. Huber, O. Y. Ovchinnikova, R. Cadalbert, J. Wall, P. Güntert, A. Böckmann, R. Glockshuber, B. H. Meier. Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation. Angew. Chem. Int. Ed. Engl. 54, 331-335 (2015) >>
K. O. Tan, M. Rajeswari, P. K. Madhu, M. Ernst. Asynchronous symmetry-based sequences for homonuclear dipolar recoupling in solid-state nuclear magnetic resonance. J. Chem. Phys. 142, 065101 (2015) >>
M. L. Fogeron, A. Badillo, V. Jirasko, J. Gouttenoire, D. Paul, L. Lancien, D. Moradpour, R. Bartenschlager, B. H. Meier, F. Penin, A. Böckmann. Wheat germ cell-free expression: Two detergents with a low critical micelle concentration allow for production of soluble HCV membrane proteins. Protein Expr. Purif. 105, 39-46 (2015) >>
B. H. Meier, A. Böckmann. The structure of fibrils from "misfolded" proteins. Curr. Opin. Struct. Biol. 30C, 43-49 (2015) >>
V. Agarwal, S. Penzel, K. Szekely, R. Cadalbert, E. Testori, A. Oss, J. Past, A. Samoson, M. Ernst, A. Böckmann, B. H. Meier. De Novo 3D Structure Determination from Sub-milligram Protein Samples by Solid-State 100 kHz MAS NMR Spectroscopy. Angew. Chem. Int. Ed. Engl. 53, 12253-12256 (2014) >>
K. O. Tan, A. B. Nielsen, B. H. Meier, M. Ernst. Broad-band DREAM recoupling sequence. J. Phys. Chem. Lett. 5, 3366-3372 (2014) >>
K. B. Sai Sankar Gupta, E. Daviso, G. Jeschke, A. Alia, M. Ernst, J. Matysik. Spectral editing through laser-flash excitation in two-dimensional photo-CIDNP MAS NMR experiments. J. Magn. Reson. 246, 9-17 (2014) >>
N. Luckgei, A. K. Schütz, B. Habenstein, L. Bousset, Y. Sourigues, R. Melki, B. H. Meier, A. Böckmann. Solid-state NMR spectral assignments of the amyloid core of Sup35pNM. Biomol. NMR Assign. 8, 365-370 (2014) >>
A. Sigfridsson, K. Weiss, L. Wissmann, J. Busch, M. Krajewski, M. Batel, G. Batsios, M. Ernst, S. Kozerke. Hybrid Multiband Excitation Multiecho Acquisition for Hyperpolarized 13C Spectroscopic Imaging. Magn. Reson. Med. In press >>
A. K. Schütz, B. Habenstein, N. Luckgei, L. Bousset, Y. Sourigues, A. B. Nielsen, R. Melki, A. Böckmann, B. H. Meier. Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p. Biomol. NMR Assign. 8, 349-356 (2014) >>
J. Gath, L. Bousset, B. Habenstein, R. Melki, B. H. Meier, A. Böckmann. Yet another polymorph of alpha-synuclein: solid-state NMR sequential assignments. Biomol. NMR Assign. 8, 395-404 (2014) >>
S. K. Jain, A. B. Nielsen, M. Hiller, L. Handel, M. Ernst, H. Oschkinat, Ü. Akbey, N. Chr. Nielsen. Low-power polarization transfer between deuterons and spin-1/2 nuclei using adiabatic RESPIRATIONCP in solid-state NMR. Phys. Chem. Chem. Phys. 16, 2827-2830 (2014) >>
M. Batel, A. Däpp, A. Hunkeler, B. H. Meier, S. Kozerke, M. Ernst. Cross-polarization for dissolution dynamic nuclear polarization. Phys. Chem. Chem. Phys. 16, 21407-16 (2014) >>
B. Kunert, C. Gardiennet, D. Lacabanne, D. Calles-Garcia, P. Falson, J.-M. Jault, B. H. Meier, F. Penin, A. Böckmann. Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studies. Front. Mol. Biosci., 1, 1-11 (2014) >>
A. Daskalov, M. Gantner, M. A. Waelti, T. Schmidlin, C. N. Chi, C. Wasmer, A. Schuetz, J. Ceschin, C. Clave, S. Cescau, B. Meier, R. Riek, S. J. Saupe. Contribution of Specific Residues of the beta-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability. PLoS Pathog.10, e1004158 (2014) >>
J. J. Wittmann, L. Hendricks, B. H. Meier, M. Ernst. Controlling spin diffusion by tailored rf-irradiation schemes. Chem. Phys. Lett. 608, 60-67 (2014) >>
N. Luckgei, B. Habenstein, F. Ravotti, S. Megy, F. Penin, J. B. Marchand, F. Hill, A. Böckmann, B. H. Meier. Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein. Biomol NMR Assign. 8, 1-6 (2014) >>
J. Gath, L. Bousset, B. Habenstein, R. Melki, A. Böckmann, B. H. Meier. Unlike twins: An NMR comparison of two alpha-synuclein polymorphs featuring different toxicity. PLoS One 9, e90659 (2014) >>
M. Huber, O. Y. Ovchinnikova, A. K. Schütz, R. Glockshuber, B. H. Meier, A. Böckmann. Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (Aβ1-40 E22Δ) fibrils. Biomol. NMR Assign. In press. >>
K. O. Tan, I. Scholz, J. D. van Beek, B. H. Meier, M. Ernst. Improved decoupling during symmetry-based C9-TOBSY sequences. J. Magn. Reson. 239, 61-68 (2014) >>