The National Institute of Diabetes & Digestive & Kidney Diseases

Development of new techniques and approaches for determining the structure and dynamics of bioactive molecules. The four main areas of interest comprise:

(A) Development of methods for improving the accuracy of biomolecular structures determined by NMR data. Emphasis is on the development of better measurement techniques for interproton distances and dihedral angles from NOEs and J couplings, and development of a quantitative relation between molecular structure and chemical shifts/chemical shift anisotropy.

(B) Development of methods for characterizing 'long-range' intramolecular order by the measurement of dipolar couplings and rotational diffusion anisotropy. This addresses the main shortcoming of conventional NMR methods, which only provide strictly local structural constraints.

(C) Study of the relation between protein mobility and function by NMR methods.

(D) Development of techniques to extend the molecular weight limit of NMR structure determination.

The Bax Group home page.

1. Delaglio F, Kontaxis G, Bax A. Protein structure determination using molecular fragment replacement and NMR dipolar couplings. Journal of the American Chemistry Society(122): 2142-2143, 2000.

2. Cornilescu G, Ramirez BE, Frank MK, Clore GM, Gronenborn AM, Bax A. Correlation between 3hJNC' and hydrogen bond length in proteins. Journal of the American Chemistry Society(121): 6275-6279, 1999.

3. Tjandra N Bax A  Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium.  Science (278): 1111-4, 1997. [Full Text/Abstract]

4. Barbato G Ikura M Kay LE Pastor RW Bax A  Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible.  Biochemistry (31): 5269-78, 1992. [Full Text/Abstract]

5. Ikura M Kay LE Bax A  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): 4659-67, 1990. [Full Text/Abstract]