Pittsburgh Spectroscopy Award
Tuesday, March 15th, 2011
2:00 PM Room: 312B

Allen J Sharkins, The Pittsburgh Conference

2:00 PMIntroductory Remarks -
2:05 PMPresentation
2:10 PMThe Sticky Fingers of Influenza Visualized by Modern Solution NMR, Adriaan Bax
2:45 PMMagic Angle Spinning Solid State NMR Structural Studies of Proteins Modified with Paramagnetic Tags, Christopher Jaroniec
3:20 PMRecess
3:35 PMSolution NMR Studies of Mitochondrial Carriers, James Chou
4:10 PMNew NMR Methods for Structural Studies of Larger RNAs, Michael Summers

Adriaan Bax of the National Institutes of Health, will receive the 2011 Pittsburgh Spectroscopy Award, presented by the Spectroscopy Society of Pittsburgh (SSP). The SSP Award, established in 1957, honors an individual who has made outstanding contributions to the field of spectroscopy.

Adriaan (Ad) Bax received his Ph.D. in 1981 from the Delft University of Technology, The Netherlands, for work related to the development of two-dimensional nuclear magnetic resonance (NMR) techniques, which he carried out at Delft and Oxford Universities. His Ph.D. thesis was reprinted in book format and for many years served as a popular text, introducing students to the application of two-dimensional NMR in chemistry. After post-doctoral work in solid-state NMR, Bax joined NIH where he currently holds the title NIH Distinguished Investigator. His work focuses on the development and application of a wide variety of advanced multi-dimensional NMR techniques to problems of biochemical and biomedical interest. Advances in the studies of proteins, pioneered by him and his group include the development of high-sensitivity indirect detection methods for 13C and 15N; the development of an approach to characterize the 15N amide motions in proteins at high sensitivity; the development of 13C/15N/1H-based triple resonance multi-dimensional NMR to assign resonances in proteins; the introduction of heteronuclear three- and four-dimensional spectroscopy for the study of protein structure; the introduction of uniform perdeuteration of proteins for the purpose of improving resolution and sensitivity of triple resonance NMR spectra; the introduction of technology that imposes a weak degree protein alignment permitting the measurement of residual dipolar couplings; and the introduction of advanced procedures that make it possible to model protein structures on the basis of chemical shifts. He and his group have applied their novel technology to a range of biomedically important systems, including the regulation of kinases by calmodulin, the structures of HIV proteins such as Nef and the catalytic core domain of integrase, the Parkinson's disease related protein alpha-synuclein, and the fusion domain of influenza virus protein hemagglutinin.

Bax’s work has been recognized by numerous awards, including the Maryland Outstanding Young Scientist Award from the Maryland Academy of Sciences, the Gold Medal from the Dutch Chemical Society, the Bijvoet Medal from Utrecht University, the Protein Society Young Investigator Award, the E. Bright Wilson, Hillebrand, and Remsen Awards from the American Chemical Society, the Kirkwood Medal from Yale University, the Gunther Laukien Award from the Experimental NMR Conference, the John Scott Award from the City of Philadelphia, the Jeanette Piperno Award from Temple University, the Hans Neurath Award from the Protein Society, and the Glenn Seaborg Medal from UCLA, and the City of Florence Award for the Molecular Sciences. He holds an honorary doctorate from the Free University of Brussels, is a corresponding member of the Dutch Royal Academy of Sciences, a Fellow of the American Academy of Arts and Sciences, a competing member of DC Velo, and a Member of the National Academy of Sciences.