Ad Bax

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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)
Website
spin.niddk.nih.gov/bax

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.

Biography[edit]

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. 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.[1]

Work in NMR spectroscopy[edit]

Bax works in the field of biomolecular NMR spectroscopy, and he has developed many of the standard methods in the field. Bax is a pioneer in the development of triple resonance experiments and technology for resonance assignment of isotopically-enriched proteins.[2][3] He was also heavily involved in the development of using residual dipolar couplings[4] and chemical shifts[5] for determining RNA[6] and protein structures.[7] Recent work focuses on the roles of proteins in membranes [8] [9] [10] .

He is one of the most cited and important scientists in the field of biomolecular NMR.[11]

References[edit]

  1. ^ "Book of Members, 1780-2010: Chapter B". American Academy of Arts and Sciences. Retrieved May 28, 2011. 
  2. ^ Ikura M, Kay LE, Bax A (1990). "A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.". Biochemistry 29 (19): 4659–67. doi:10.1021/bi00471a022. PMID 2372549. 
  3. ^ Lewis E Kay, Mitsuhiko Ikura, Rolf Tschudin, Ad Bax (1990). "Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins". Journal of Magnetic Resonance 89 (3): 496–514. Bibcode:1990JMagR..89..496K. doi:10.1016/0022-2364(90)90333-5. 
  4. ^ Tjandra N, Grzesiek S, Bax A (1996). "Magnetic field dependence of nitrogen-proton J splittings in 15N-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling". Journal of the American Chemical Society 118: 6264–6272. doi:10.1021/ja960106n. 
  5. ^ Kontaxis G, Delaglio F, Bax A (2005). "Molecular fragment replacement approach to protein structure determination by chemical shift and dipolar homology database mining". Methods in Enzymology 394: 42–78. doi:10.1016/s0076-6879(05)94003-2. 
  6. ^ Boisbouvier A, Delaglio F, Bax A (2003). "Direct observation of dipolar couplings between distant protons in weakly aligned nucleic acids". Proceedings of the National Academy of Sciences USA 100: 11333–11338. Bibcode:2003PNAS..10011333B. doi:10.1073/pnas.1534664100. 
  7. ^ Bax A, Grishaev A (October 2005). "Weak alignment NMR: a hawk-eyed view of biomolecular structure". Curr. Opin. Struct. Biol. 15 (5): 563–70. doi:10.1016/j.sbi.2005.08.006. PMID 16140525. 
  8. ^ Maltsev AS, Chen J, Levine RL, Bax A (February 2013). "Site-specific interaction between α-synuclein and membranes probed by NMR-observed methionine oxidation rates". J. Am. Chem. Soc. 135 (8): 2943–6. doi:10.1021/ja312415q. PMC 3585462. PMID 23398174. 
  9. ^ Lorieau JL, Louis JM, Bax A (March 2013). "The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics". Biopolymers 99 (3): 189–95. doi:10.1002/bip.22102. PMID 23015412. 
  10. ^ Lakomek NA, Kaufman JD, Stahl SJ, Louis JM, Grishaev A, Wingfield PT, Bax A (April 2013). "Internal dynamics of the homotrimeric HIV-1 viral coat protein gp41 on multiple time scales". Angew. Chem. Int. Ed. Engl. 52 (14): 3911–5. doi:10.1002/anie.201207266. PMID 23450638. 
  11. ^ Citation Laureates: Chemistry

External links[edit]