An Approach to the Structure Determination of Larger Proteins Using Triple Resonance NMR Experiments in Conjunction with Random Fractional Deuteration

Autor:	R. William Broadhurst, Mark J. S. Kelly, Yutaka Ito, James Keeler, Daniel Nietlispach, and Peter J. Domaille, Robin T. Clowes, Hartmut Oschkinat, Jennifer Ashurst, Ernest D. Laue
Rok vydání:	1996
Předmět:	Colloid and Surface Chemistry Nuclear magnetic resonance Chemistry Resonance General Chemistry Sensitivity (control systems) Biochemistry Two-dimensional nuclear magnetic resonance spectroscopy Catalysis
Zdroj:	Journal of the American Chemical Society. 118:407-415
ISSN:	1520-5126 0002-7863
DOI:	10.1021/ja952207b
Popis:	A combination of simulation and experiment is used to demonstrate that the sensitivity of a family of 3D/4D NMR experiments used to assign resonances and to obtain structural restraints in proteins is improved by partial random deuteration; the improvement increases as the correlation time of the protein becomes longer. The results suggest that deuteration at a level of ∼50% optimizes the sensitivity of experiments which are used to assign sidechain 1H and 13C resonances by correlating them with the resonances from backbone nuclei. In addition, this level of deuteration is also a good compromise for recording NOESY experiments. Using this approach, it should be possible to determine structures of larger proteins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::006aa79a45a90c1c0cc4ef01b784179e https://doi.org/10.1021/ja952207b Zobrazit plný text záznamu