We have continued our study of biological macromolecules dissolved in a very dilute, nematic liquid crystalline (LC)phase. Various improvements to the original phospho lipid based medium have been made which extend the original 5.5-7.5 pH range to 2-11, and the temperature range which originally was 30-40Chas been increased to 20-50C, which makes the technology applicable to the majority of systems of interest. We have shown that measurement of dipolar couplings in the LC phase provides extremely precise structural information, which allows characterization of the relative, libration-averaged effective internuclear distances and angles. We have shown that measurement of dipolar couplings can provide a rapid means for evaluating the agreement between the prevalent solution structure and a structural model, and have also developed methods for improving the accuracy of structures calculated from NMR data. Most of this work has focused on a small model protein, ubiquitin, which has been well characterized by crystallographic and previous NMR studies. The methodology is also being tested on a variety of other systems, including a DNA dodecamer, the V-alpha domain of the human T-cell receptor, and DinI, a protein involved in shutting down the SOS response. - NMR, protein structure, liquid crystal, micelle, bicelle, magnetic alignment

National Institute of Health (NIH)
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Intramural Research (Z01)
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Lee, Jung Ho; Ying, Jinfa; Bax, Ad (2016) Quantitative evaluation of positive ? angle propensity in flexible regions of proteins from three-bond J couplings. Phys Chem Chem Phys 18:5759-70
Vogeli, Beat; Yao, Lishan; Bax, Ad (2008) Protein backbone motions viewed by intraresidue and sequential HN-Halpha residual dipolar couplings. J Biomol NMR 41:17-28
Chill, Jordan H; Louis, John M; Delaglio, Frank et al. (2007) Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR. Biochim Biophys Acta 1768:3260-70
Ying, Jinfa; Chill, Jordan H; Louis, John M et al. (2007) Mixed-time parallel evolution in multiple quantum NMR experiments: sensitivity and resolution enhancement in heteronuclear NMR. J Biomol NMR 37:195-204
Grishaev, Alexander; Ying, Jinfa; Bax, Ad (2006) Pseudo-CSA restraints for NMR refinement of nucleic acid structure. J Am Chem Soc 128:10010-1
Ying, Jinfa; Grishaev, Alexander; Bryce, David L et al. (2006) Chemical shift tensors of protonated base carbons in helical RNA and DNA from NMR relaxation and liquid crystal measurements. J Am Chem Soc 128:11443-54
Ying, Jinfa; Bax, Ad (2006) 2'-hydroxyl proton positions in helical RNA from simultaneously measured heteronuclear scalar couplings and NOEs. J Am Chem Soc 128:8372-3
Chill, Jordan H; Louis, John M; Miller, Christopher et al. (2006) NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci 15:684-98
Ying, Jinfa; Grishaev, Alexander; Bax, Ad (2006) Carbon-13 chemical shift anisotropy in DNA bases from field dependence of solution NMR relaxation rates. Magn Reson Chem 44:302-10
Dam, Julie; Baber, James; Grishaev, Alexander et al. (2006) Variable dimerization of the Ly49A natural killer cell receptor results in differential engagement of its MHC class I ligand. J Mol Biol 362:102-13

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