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| Name |
Bax, Adriaan |
| Location
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National Institutes of Health |
| Primary Field
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Biophysics and Computational Biology |
| Secondary Field
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Chemistry |
 Election Citation
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Bax has been one of the pioneers in the development of nuclear magnetic resonance spectroscopy, abbreviated as NMR. This technique is widely used to determine the atomic structure of molecules, including the motions and three-dimensional structures of proteins. He has created some of the newest methods of high-resolution NMR spectroscopy and used these techniques to extend our abilities to probe protein structure and function. |
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Research Interests
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My research has been primarily on the development and application of nuclear magnetic resonance (NMR) methods for studying the structure and dynamics of proteins. Our so-called triple resonance approach relies on uniform 13C and 15N enrichment of proteins, and utilizes through-bond J couplings to assign the various resonances. By extending the original concept of two-dimensional NMR to three and even four dimensions, the resonance overlap problem was greatly reduced, thereby significantly increasing the size of proteins accessible by NMR. Further extension of this limit became feasible when we combined perdeuteration of the non-exchangeable hydrogens with the triple resonance concept. The incorporation of stable 15N and 13C isotopes into proteins also permitted us to develop straightforward ways for the quantitative study of protein backbone dynamics. Much of this early work was on the regulatory protein calmodulin and on the relative mobility of its two domains. More recently, after I succeeded in aligning proteins in dilute liquid crystalline suspensions, we were able to measure dipole-dipole couplings that define orientations of bond vectors relative to a common reference frame. This not only provides a unique structure validation tool but also can increase dramatically the global accuracy of NMR structures. My current interest focuses on the use of dipolar couplings to further accelerate the structure determination process and to extend NMR to lipophilic proteins. |
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