CALL FOR NOMINATIONS - Deadline is October 31
The Laukien Prize was established in 1999 to honor the memory of Professor Gunther Laukien, a co-founder of Bruker. The Laukien Prize carries a monetary award of $20,000 funded by Bruker and is intended to recognize cutting-edge experimental NMR research with a high probability of enabling beneficial new applications. The Prize recipient will also deliver the opening Plenary lecture at the ENC conference.
View listing of Past Recipients of the Gunther Laukien Prize
Nominations for the Laukien Prize are now being accepted. The award will be announced at the next ENC. The nominated work should be published within the last three years. In some special cases, the award may be for cumulative achievements over a longer period.
Nominations should include the following and be submitted by October 31:
- Name of nominee, the nominee's affiliation, address, phone, fax and e-mail.
- Name of nominator, address, phone, fax and e-mail.
- A brief (no more than 200 words) description of the work serving as the basis for the nomination.
- A list of relevant publications (no more than 5).
- By email to email@example.com
- By mail or courier to: ENC - Laukien Prize | 2019 Galisteo Street, Bldg i-1 | Santa Fe, NM 87505 (USA)
2018 LAUKIEN PRIZE RECIPIENT
Bob Griffin (left) pictured with recipient Gerhard Wagner (right)
Gerhard Wagner was born in 1945 in Bor, Czech Republic and grew up in Southern Bavaria. During his undergraduate years he studied physics at the Technische Universität of Munich, graduating in 1972 with a Diploma thesis on Mössbauer spectroscopy of iron containing proteins. Thereafter, he decided to pursued a Ph.D. at the ETH Zurich under the guidance of Professor Kurt Wüthrich. His initial effort was to understand the NMR spectrum of the basic pancreatic trypsin inhibitor, BPTI. At the outset it was not clear what could be learned from this endeavor !
His initial efforts were directed at understanding the phenomenon of amide hydrogen/deuterium exchange as a tool to understand protein breathing dynamics with residue specific resolution. However, this required sequence specific resonance assignments, which were not yet available. Thus, he focused on the resonances of the aromatic side chains and discovered that aromatic rings flip rapidly even in the most rigid proteins. The rates of these processes and their temperature and pressure dependence can be measured quantitatively by NMR. Importantly, Wagner’s data provided an initial test bed for the development of molecular dynamics calculations. In a parallel effort, he studied protein dynamics with hydrogen-deuterium exchange at limits of uncorrelated (EX2) and correlated (EX1) exchange. Quantitative analysis of exchange rates indicated that exchange of the innermost amides required complete unfolding of BPTI. In 1977 he obtained his Ph.D. with a thesis on NMR studies of protein dynamics.
Subsequently, Gerhard joined the group of Professor John Waugh at MIT for a short postdoctoral stay to explore the potential of solid state NMR for protein studies. In 1979 he returned to the ETH and established a technology for sequential resonance assignments based on 1D NOE and spin decoupling, which allowed assignment of all slowly exchanging amides in the -sheet secondary structures of BPTI. With the introduction of 2D NMR methods he quickly assigned the entire spectrum of BPTI, which was the first complete NMR assignment for any protein. The technology he developed formed the basis for the first solution NMR structures of proteins.
In 1986, prior to moving to the University of Michigan, Wagner initiated construction of a triple resonance probe to enable precise measurements of homonuclear couplings by observing HN-C cross peaks without flipping the H between evolution and detection periods. He discovered this possibility when measuring H-H cross peaks of 113Cd-bound cysteines in the protein metallothionein. In addition, in 1988, when executing the experiment with G. Montelione on a small 15N labeled peptide and natural abundance 13C, he discovered sequential cross peaks connecting amides with the C of the preceding residues. This was essentially the first HNCA type experiment, and a feature now used extensively in triple-resonance assignments of proteins.
In 1990 Dr. Wagner was recruited to Harvard Medical School where he focused on protein dynamics and developed procedures for mapping of spectral density functions. However, he became increasingly focused on revealing mechanistic aspects of proteins involved in important biological problems. Currently he is interested in understanding mechanisms of human translation initiation, transcriptional activation mediated by activator co-activator interactions, T-cell activation, non-ribosomal peptide synthesis and membrane protein structure. He has determined more than 50 unique structures of proteins in solution. A major current effort is focused on the discovery and characterization of small molecule inhibitors of protein-protein interactions that might have therapeutic use in curing human disease.
Despite the focus on biological problems, Dr. Wagner continues to be strongly interested in the further development of NMR methods. This includes procedures for advanced sampling and data reconstruction. Another recent focus is on exploiting the TROSY effect while detecting low- nuclei in solution NMR spectroscopy.