The Gunther Laukien Prize is awarded annually at the Experimental NMR Conference (ENC) to recognize cutting-edge NMR research which shows a high probability of enabling new applications. This year’s 2017 Prize was awarded to Kurt Zilm and Bernd Reif for their independent pioneering development of 1H-detected magic angle spinning (MAS) experiments and numerous other solid-state NMR applications and methods.
Due to their high gyromagnetic ratio and natural abundance, protons ( 1H’s) offer a considerably increase in NMR spectral sensitivity compared to the detection of low-g species such as 13C or 15N . However, direct 1H detection in solid state NMR was long considered impractical due to strong 1H-1H dipole coupling that results in broad spectral lines and is not attenuated by MAS. Reif and Zilm addressed this problem by performing experiments on sparse 1H’s embedded in a perdeuterated matrix, eliminating the 1H-1H dipolar broadening and demonstrating the critical role of 1H detection for biomolecular NMR. These seminal experiments, first reported in 2003, opened new regimes to biomolecular NMR dynamics and, because of the associated gains in sensitivity and resolution, considerably extended its capabilities for structure determination,. As a result, 1H detection was quickly recognized as an essential tool for MAS NMR and this has provided the motivation for the development of new instrumentation and methods for higher MAS frequencies. Higher spinning frequencies in turn eliminated the requirement that the samples be perdeuterated to observe high resolution.. Today, 1H detected MAS experiments are setting new standards for the study of proteins by solids NMR. The exciting current developments employed at wr/2p >100 kHz are based on the groundbreaking work of Reif and Zilm.
Introduction of Laukien Prize Winners by Bob Griffin, MIT
Watch this video to learn the history of the Laukien Prize and hear the introductions of the winners during the presentations at ENC. Introduction to Laukien Prize and Recipients,
Bernd Reif, Technische Universität München
Dr. Reif began his career at the University of Frankfurt, Germany where he worked with Christian Griesinger developing solution NMR methods to determine the structure of biomacromolecules, natural products and metal organic molecules. He then joined Robert Griffin’s group at MIT where he implemented the first 1H‑detected solids experiment using a perdeuterated peptide sample. Following work at the Leibniz-Institut fur Molekulare Pharmakologie in Berlin and Charité – Universitätsmedizin Berlin, Dr. Reif accepted a faculty position at Technische Universitat Munchen where he is currently a faculty member in the Department of Chemistry.
Dr. Reif demonstrated an important breakthrough in the investigation of perdeuterated micro-crystalline protein samples re-crystallized from a buffer containing large amounts of D20, leading to 1H detected 1H, 15N MAS correlation spectra with a resolution comparable to that achieved through solution-state NMR. 1H spin dilution facilitates the quantification of 1H-1H distances in a protein and contributed to the feasibility of 1H detection, which would otherwise have suffered from broad spectral lines using the MAS rates available at the time. The presence of isolated spin pairs also enables the characterization of dynamic processes that are not affected by spin-diffusion. Side chain protons can be detected with high sensitivity and resolution, using specific 1H-labeled amino acid precursors for bacterial growth.
In addition, Dr. Reif and colleagues demonstrated that 2H nuclei in the side chains can be employed to yield high-resolution 2H, 13C correlation spectra and to retrieve unique dynamics information from 2H relaxation in these uniformly labeled samples. Furthermore, they were able to show that solid-state TROSY effects yield spectral benefits in 1H,15N correlations for residues that undergo dynamics in the ms-us timescale. With this, 1H‑detected experiments were developed and applied to the membrane proteins bacteriorhodospin and OmpG, as well as for fibrils formed by the Aβ peptide.
Kurt W. Zilm, Yale University
Dr. Zilm studied chemistry and chemical engineering at the University of Utah and completed his Ph.D. research under the late David M. Grant, and did contract research for energy exploration and petrochemical companies. Following an appointment at the National Bureau of Standards and U.C. Berkeley, Dr. Zilm moved to Yale where he continues his distinguished career. He has won numerous awards and served the magnetic resonance community through membership on the ENC executive committee for 12 years, as ENC chair in 2006, as chair of the magnetic resonance GRC in 2003 and chair of the Rocky Mountain Conference since 2005.
Throughout his career, Dr. Zilm has developed a variety of NMR methods and instrumentation to study an array of chemical problems. His early work applied 13C MAS NMR to organic source rocks, model hydrocarbons and synthetic polymers. He developed some of the first spectral editing methods for MAS NMR. While still a graduate student, he designed and constructed a probe where the sample was cooled with a closed-cycle He refrigerator for 13C NMR of small molecules in argon matrices at 10 K. He developed a 77 K MAS probe to study reactive intermediates and small molecules absorbed on the surface of supported metal catalysts while at Yale. His group has used NMR to study unusual chemical structures and bonding, discovering quantum mechanical proton-exchange couplings in transition metal polyhydrides and measuring metal dihydrogen complexes.
Dr. Zilm was a pioneer in the development of solid-state protein NMR in the late 1990’s, using isotopically enriched nano-crystalline samples, fast MAS and high fields. His group made significant contributions to sample prep methods and introduced the use of tuning tube elements and balanced rf circuits in MAS probes. Dr. Zilm was involved in the early sequential assignments of proteins in the solid state, collaborating with Ann McDermott and Andy Byrd. His group was a pioneer in the use of perdeuteration in solid-state protein NMR, making it possible to obtain distance constraints between amide protons, to perform site resolved relaxation studies of motions in peptides and proteins and to observe high resolution amide 1H NMR spectra for proteins. Dr. Zilm’s group performed one of the earliest demonstrations of high resolution 1H detected 2D NMR in perdeuterated back-exchanged proteins.
1H detected experiments are currently performed at MAS frequencies of 100 kHz and above with fully protonated samples. Dr. Reif’s and Zilm’s experiments, are the foundation of 1H detection and provided the scientific impetus for the development of today’s very fast MAS probes.
The Laukien Prize and Bruker BioSpin’s Commitment to Supporting Research
We at Bruker BioSpin recognize the key value of this combined body of research. Both Dr. Zilm and Dr. Reif have played essential roles in stimulating developments in solid-state NMR and in building its legacy of unique insights for biomolecular applications. Their ground-breaking work pushed researchers at Bruker BioSpin and beyond to achieve MAS rates of 111 kHz. Altogether, the community now has access to methods and instruments that are expanding the body of knowledge for structure and dynamics of biomolecular systems that were previously inaccessible. Rapid progress continues in these areas, as Bruker Biospin works closely with the community of researchers, exemplifying our commitment to “improving life through innovating science”.
Enjoy these photos from the Laukien Prize ceremony