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Ad
Bax received his Ph.D. in 1981 from the Delft University of Technology,
The Netherlands, for work related to development of two-dimensional
nuclear magnetic resonance (NMR) techniques, which he carried
out at Delft and Oxford Universities.
After post-doctoral work in solid-state
NMR with Gary Maciel at Colorado State University, he joined
NIH where he has been working on the development and application
of a wide variety of advanced multi-dimensional NMR techniques.
Initially, this work focused on the study of natural products
and other small molecules, but in the latter half of the eighties
he extended these techniques to study the three-dimensional structure
and dynamic properties of proteins. This work exploits advances
in molecular biology, which make it possible to over-express
most proteins in E. coli bacteria, permitting the incorporation
of 13C and 15N stable isotopes.
Based on the availability of these stable
isotopes, Bax and co-workers developed more efficient procedures
for obtaining complete resonance assignments of proteins. Moreover,
the isotopes permitted them to increase spectral resolution by
dispersing the complex NMR spectra in up to four orthogonal frequency
dimensions. This minimizes resonance overlap and allows a far
more detailed study of the numerous internuclear interactions
than was possible before. These interactions provide information
not only on the time-averaged three-dimensional structure of
a protein, but also on the amplitude and time scale of structural
fluctuations.
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Most recently, the Bax group developed
a method for weakly aligning biological macromolecules with respect
to the magnetic field by using a nematic liquid crystalline solution
of large particles. The very weak degree of orientation thereby
imposed on the solute molecules ensures that the NMR spectrum
retains its simple, solution-state character, but nevertheless
is sufficiently large to permit measurement of direct dipole-dipole
couplings. These couplings provide information on the time-averaged
orientation of the corresponding internuclear vector relative
to the magnetic field, and thereby on the orientation of vectors
relative to one another. This information is intrinsically different
in character from that conventionally extracted from solution
NMR spectra, and holds promise both for improving the accuracy
of NMR structure determination, and for extending the size limit
of proteins and nucleic acids that can be studied by NMR.
Ad Bax has received 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 John Scott Award from the City of Philadelphia, the Jeanette
Piperno Award from Temple University, the Hans Neurath Award
from the Protein Society, and he is a corresponding member of
the Dutch Royal Academy of Sciences, a Fellow of the American
Academy of Arts and Sciences, and a Member of the National Academy
of Sciences.
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