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).
ENC - Laukien Prize
2019 Galisteo Street, Bldg i-1
Santa Fe, NM 87505 (USA)
2017 LAUKIEN PRIZE RECIPIENTS
Frank Laukien (center) pictured with recipients Bernd Reif (left) and Kurt Zilm (right)
Bernd Reif (Technische Universität München) was born in 1968 in Hof/Saale, Germany. As an undergraduate he studied physics and biochemistry at the Universität of Bayreuth. In 1998 he completed his PhD at the Universität Frankfurt in chemistry where he worked together with Prof. Christian Griesinger on the development of novel NMR methods for determining the structure of biomacromolecules, natural products and metal organic molecules. Among his research projects, were efforts to develop 1H detected versions of the INADEQUATE experiment to improve the sensitivity of solution spectra of natural products.
Many methodological developments in solution-state NMR have roots in solid-state experiments, and, accordingly, Dr. Reif joined the group of Prof. Robert G. Griffin at MIT as a postdoctoral fellow. During this time, he implemented the initial 1H detected experiments using a perdeuterated peptide sample. After his postdoctoral fellowship, Dr. Reif lead an Emmy-Noether research group at the Technische Universität München (TUM), with projects directed at combining solution-state and solid-state NMR to characterize biomolecular systems that are difficult to access in solution. In 2001, Bernd initiated a collaboration with Prof. Hartmut Oschkinat's group involving 1H detection using micro-crystalline protein preparations of the α-spectrin SH3 domain.
From 2003 to 2010, Dr. Reif was a group leader at the Leibniz-Institut für Molekulare Pharmakologie (FMP) in Berlin. In 2004, he became a professor at the Charité Universitätsmedizin Berlin. In 2010, Dr. Reif accepted a faculty position in the Department of Chemistry at the TUM, and at the Helmholtz-Zentrum München in Neuherberg.
A break-through of his research was the investigation of perdeuterated micro-crystalline protein samples re-crystallized from a buffer containing large amounts of D2O which lead to the initial 1H detected 1H,15N MAS correlation spectra, with a resolution comparable to the resolution achieved by solution-state NMR. 1H spin dilution facilitates the quantification of 1H-1H distances in a protein. The presence of isolated spin pairs enables the characterization of dynamic processes that are not affected by spin-diffusion. Side chain 1H’s can be detected with high sensitivity and resolution, using specifically 1H labeled amino acid precursors for bacterial growth.
In the spin dilution approach, deuteration is primarily employed to decrease the 1H spin density. However, Reif and coworkers showed that 2H’s in the side chains can be employed to yield high-resolution 2H,13C correlation spectra, and to retrieve dynamics information from 2H in these uniformly labeled samples. Subsequently, the Reif group demonstrated that TROSY like experiments yield beneficial spectral properties for residues that undergo dynamics in the ns-μs timescale. Over the years, 1H detected experiments were developed further and applied in his group to the membrane proteins bacteriorhodopsin and OmpG, as well as for fibrils formed by the Alzheimer's disease Aβ peptide.
Currently, 1H detected experiments are performed at MAS frequencies at 100 kHz and above using fully protonated samples. The experiments involving deuterated peptides and proteins introduced by Reif and colleagues served to nucleate the field of 1H detection in the solid-state and provided the impetus for the development of MAS probes that achieve r/2>100 kHz.
Dr. Reif's current research focuses on the development of MAS solid-state NMR methods for the characterization of structural and dynamical properties of proteins in the solid-state. Experiments include application of solution- and solid-state NMR spectroscopy to the study of amyloidogenic peptides and membrane proteins, with emphasis on the characterization of Aβ fibril structure, as well as the analysis of the interference of amyloids with small molecules and chaperones, such as the small heat shock protein αB-crystallin.
Kurt W. Zilm (Yale University) was born in 1955 in Des Moines, Iowa. He received his B.S. (1976) and Ph.D. degrees (1981) from the University of Utah, where he studied under the late David M. Grant. His independent research career began at the University of Utah Research Institute where he did contract research for major energy exploration and petrochemical companies. Following an appointment as a visiting scientist at the National Bureau of Standards with David Vanderhart, and a postdoc at U.C. Berkeley with Alex Pines, Kurt moved to Yale in 1983 where he has been Professor of Chemistry since 1993. His work has been recognized by awards including the Franz-Vögt Prize of the Justus-Liebig University, election as a fellow of the AAAS, and in 2014 election to the Connecticut Academy of Sciences. Kurt has a long record of service to the magnetic resonance community, sitting on the ENC executive committee for 12 years, serving as ENC chair in 2006, chair of the magnetic resonance GRC in 2003, and as chair of the Rocky Mountain Conference on Magnetic Resonance since 2005.
During his career Kurt has developed a variety of new NMR methods and instrumentation, and used them to study a diverse array of chemical problems. His early work applied 13C MAS NMR to organic source rocks, model hydrocarbons and synthetic polymers, and developed some of the first spectral editing methods for MAS NMR. As a graduate student he built an NMR probe where the sample was cooled with a closed cycle He refrigerator for 13C NMR of small molecules in argon matrices at 10 K. At Yale he developed a 77 K MAS NMR probe to study reactive intermediates such as singlet biradicals trapped in hydrocarbon matrices, and small molecules absorbed on the surface of supported metal catalysts. His group has used NMR to study unusual chemical structures and bonding, for instance determining the strength of the Sn=Sn bond by NMR, discovering quantum mechanical proton exchange couplings in transition metal polyhydrides, and measuring H-H bond lengths and rotation barriers in transition metal dihydrogen complexes. Kurt has also worked on hyperpolarized Xe, carrying out early experiments where the optical pumping was performed in the same high magnetic field used for NMR detection.
Beginning in the late 1990's, Kurt was a pioneer in the development of solid state protein NMR using isotopically enriched nano-crystalline samples, fast MAS, and high magnetic fields. His group made important contributions to sample preparation methods and introduced the use of tuning tube elements and circuit balancing in MAS probes. Collaborating with Ann McDermott and Andy Byrd, Kurt was involved with some of the earliest sequential assignments of proteins in the solid state. His group did pioneering work in the use of perdeuteration in solid state protein NMR, making it possible to obtain distance constraints between amide 1H’s, perform site resolved relaxation studies of motions in peptides and proteins, and observe high resolution amide 1H NMR spectra for proteins. His group made one of the earliest demonstrations of high resolution 1H detected 2D NMR in perdeuterated back-exchanged proteins, which has provided much of the impetus to develop ultra-fast MAS probes for protein NMR.
Kurt's research continues to combine applications to important chemical problems with development of NMR methods and instrumentation. His present program involves NMR structural study of infectious recombinant prions, and complexes of prion protein with Aβ oligomers implicated in Alzheimer's disease. His group is also engaged in development of DNP instrumentation using frequency agile diode based millimeter-wave sources, where they are pioneering the use of novel quasi-optical and dielectric structures in the MAS probe to enable DNP enhanced MAS NMR on microliter sized samples.
In addition to his research and teaching, Kurt is the host of a popular public science outreach program, Science Saturdays at Yale (http://onhsa.yale.edu/programs/science-saturdays), now in its second decade. Kurt and his wife Velma live in Hamden, Connecticut where they enjoy maple sugaring, hiking, fishing and boating on Long Island Sound, and especially being grandparents to their granddaughter Lydia Kay.