Ad Bax
| Adriaan (Ad) Bax | |
|---|---|
| Born | Zevenbergen, Netherlands |
| Residence | United States |
| Citizenship | United States |
| Fields | Nuclear magnetic resonance, biophysics |
| Institutions | NIDDK, National Institutes of Health |
| Alma mater | Delft University of Technology |
| Thesis | (B.S. 1978; PhD 1981) |
| Doctoral advisor | Ray Freeman |
| Known for | Methods development for NMR, such as RDCs (Residual dipolar coupling) |
| Notable awards |
National Academy of Sciences E. Bright Wilson Award (2000) |
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Adriaan "Ad" Bax (born 1956) is a molecular biophysicist. He was born in the Netherlands and is currently a US Citizen. He is the Chief of the Section on Biophysical NMR Spectroscopy at the National Institutes of Health. He is known for his work on the methodology of biomolecular NMR spectroscopy.
Bax was born in the Netherlands. He studied at Delft University of Technology where he got his engineer's degree in 1978, and Ph.D. degree in applied physics in 1981, after spending considerable time working with Ray Freeman at Oxford University. He worked as a postdoc with Gary Maciel at Colorado State University, before joining the NIH's Laboratory of Chemical Physics in 1983. In 1994 he became correspondent of the Royal Netherlands Academy of Arts and Sciences. He is currently the Chief of the Section on Biophysical NMR Spectroscopy at NIH. In 2002 he was elected a member of the National Academy of Sciences in the section on Biophysics and computational biology and a Fellow of the American Academy of Arts and Sciences.
Bax works in the field of biomolecular NMR spectroscopy, and has been involved in the development of many of the standard methods in the field. He collaborated extensively with fellow NIH scientists Marius Clore, Angela Gronenborn and Dennis Torchia in the development of multidimensional protein NMR. Bax is a pioneer in the development of triple resonance experiments and technology for resonance assignment of isotopically-enriched proteins. He was also heavily involved in the development of using residual dipolar couplings and chemical shifts for determining RNA and protein structures. Much of his recent work focuses on the roles of proteins in membranes. He is one of the most frequently cited scientists in the field of biomolecular NMR.
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