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 Biospin 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 deadline for nominations is November 15. 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 nominees 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).
Send nominations to:
ENC - Laukien Prize
2019 Galisteo Street, Bldg i-1
Santa Fe, NM 87505 (USA)
Or email to firstname.lastname@example.org
2015 Laukien Prize Recipient
The 2015 Günther Laukien Prize is awarded to Professor Arthur G. Palmer III for his innovative and elegant solution NMR studies of protein dynamics and thermodynamics, and for his seminal contributions to elucidating molecular motions on time scales that span several orders of magnitude. His many ingenious experiments have extended the reach of NMR beyond static three-dimensional structural studies, enabling detailed insight into biomolecular function. He has further enhanced the capabilities of the solution NMR community by developing and disseminating robust software that is widely used for analyzing spin relaxation data of proteins.
Art received a B.A. in chemistry magna cum laude in 1980 from Haverford College. There he conducted undergraduate research in the photochemistry of carbonyl carbene with Prof. Colin F. Mackay. After two years working as an analytical chemist and two years teaching high school chemistry and physics, Palmer entered graduate school, first receiving an M.S. in Industrial Health from the University of Michigan in 1986 and the Ph.D. from the University of North Carolina at Chapel Hill in 1989. His doctoral research, conducted under the direction of Prof. Nancy L. Thompson, developed the technique of high order autocorrelation in fluorescence correlation spectroscopy. Palmer made the jump to NMR spectroscopy as a National Science Foundation Postdoctoral Fellow with Dr. Peter E. Wright at the Scripps Research Institute from 1989-1992. There Palmer co-developed, with Wright, Mark Rance, and John Cavanagh, the sensitivity-enhanced HSQC and related experiments and began his first developments and applications of NMR spin relaxation to characterize macromolecular dynamics. Palmer moved to the Department of Biochemistry and Molecular Biophysics at Columbia University as an Assistant Professor in 1992; he was promoted to Associate Professor with tenure in 1998 and to Professor in 2001. He currently holds the Robert Wood Johnson Jr. Chair and serves as Vice Chair of the Department of Biochemistry and Molecular Biophysics and as Associate Dean for Graduate Affairs at Columbia University Medical Center. He also is the Director of NMR Spectroscopy at the New York Structural Biology Center and served as Chair of the 42nd ENC.
Palmer is the author of 134 papers and the co-author, with John Cavanagh, Wayne J. Fairbrother, Nicholas J. Skelton, and Mark Rance, of the book “Protein NMR Spectroscopy: Principles and Practice”, now in its second edition. He also is the author of the program ModelFree, which is widely used for analysis of spin relaxation data using the Lipari-Szabo model-free formalism. Palmer uses NMR spectroscopy and molecular dynamics simulations to elucidate the coupling between conformational dynamical properties and biological functions of proteins. His research interests include development of novel methods in NMR spectroscopy, computational and theoretical analyses of protein dynamics, and applications to protein folding, molecular recognition, and catalysis. He has contributed in particular to the use of generalized order parameters for characterizing conformational entropic effects in molecular recognition, and the use of CPMG and R1 relaxation dispersion measurements for characterizing microsecond-millisecond time scale processes. Recently, he has used molecular dynamics simulations to aid in interpretation of NMR spin relaxation measurements. Palmer has long been interested in the conformational dynamic differences between mesophilic and thermophilic enzymes that contribute to differences in activity, using the ribonuclease H superfamily as a model system. Other recent applications include the mechanism of strand swapping in dimerization of cadherin cell adhesion proteins, the role of local dynamics in DNA recognition by the GCN4 bZip transcription factor, dynamic control of the order of substrate addition in the DNA-repair enzyme AlkB, and the mechanism of autoinhibition of the Crk-II signaling adapter protein. A selected set of Palmer’s publications, one per year, is provided below.
- K. A. Stafford, N. Trbovic, J. A. Butterwick, R. Abel, R. A. Friesner, and A. G. Palmer, Conformational preferences underlying reduced activity of a thermophilic ribonuclease H, J. Mol. Biol., in press (2015). doi:10.1016/j.jmb.2014.11.023.
- M. L. Gill and A. G. Palmer, Local isotropic diffusion approximation for coupled internal and overall molecular motions in NMR spin relaxation, J. Phys. Chem. B 118, 11120-11128 (2014). doi: 10.1021/jp506580c. PMCID: PMC4174990.
- Y. Li, N. Altorelli, F. Bahna, B. Honig, L. Shapiro and A. G. Palmer, Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion, Proc. Nat. Acad. Sci. USA 110, 16462–16467 (2013). doi: 10.1073/pnas.1314303110. PMCID: PMC3799306.
- P. Robustelli, K. A. Stafford, and A. G. Palmer, Interpreting protein structural dynamics from NMR chemical shifts, J. Am. Chem. Soc. 134, 6365–6374 (2012). doi: 10.1021/ja300265w. PMCID: PMC3324661.
- J.-H. Cho, V. Muralidharan, M. Vila-Perello, D. P. Raleigh, T. W. Muir, and A. G. Palmer, Tuning protein autoinhibition by domain destablization, Nat. Struct. Mol. Biol. 18, 550-555 (2011). doi:10.1038/nsmb.2039. PMCID: PMC3265570.
- Y. Li and A. G. Palmer, Narrowing of protein NMR spectral lines broadened by chemical exchange, J. Am. Chem. Soc. 132, 8856-8857 (2010). PMCID: PMC2921271.
- N. Trbovic, J. Cho, R. Abel, R. A. Friesner, M. Rance, and A. G. Palmer, Protein side-chain dynamics and residual conformational entropy, J. Am. Chem. Soc. 131, 615–622 (2009). PMCID: PMC2413295.
- P. Maragakis, K. Lindorff-Larsen, M. P. Eastwood, R. O. Dror, J. L. Klepeis, I. T. Arkin, M. Ø. Jensen, H. Xu, N. Trbovic, R. A. Friesner, A. G. Palmer, and D. E. Shaw, Microsecond molecular dynamics simulation shows effect of slow loop dynamics on backbone amide order parameters of proteins, J. Phys. Chem. B 112, 6155-6158 (2008). PMCID: PMC2805408.
- T. I. Igumenova, U. Brath, M. Akke, and A. G. Palmer, Characterization of chemical exchange using residual dipolar coupling, J. Am. Chem. Soc. 129, 13396-13397 (2007). PMCID: PMC2527592.