Direct Carbon Detection in Paramagnetic Metalloproteins To Further Exploit Pseudocontact Shift Restraints Export

@article{citeulike:5705016, abstract = {PMID: 15327280 Direct detection heteronuclear NMR allows us to drastically reduce paramagnetic contributions to the line width as compared to 1H detection. As an example, a calcium binding protein (human oncomodulin), in which one of the calcium ions was selectively substituted with Tb3+, is used. Through a variety of 13C direct detection NMR experiments, resonances were detected as close as 5.5 A from the metal ion. Pseudocontact shifts measured through 13C direct detection experiments provide structural constraints in regions of the protein where 1H resonances are broadened beyond detection through Curie relaxation (up to 16 A from the paramagnetic center).}, author = {Babini, Elena and Bertini, Ivano and Capozzi, Francesco and Felli, Isabella C. and Lelli, Moreno and Luchinat, Claudio}, citeulike-article-id = {5705016}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/ja047573m}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/ja047573m}, day = {1}, doi = {10.1021/ja047573m}, journal = {Journal of the American Chemical Society}, keywords = {carbon\_detection, nmr, pre}, month = {September}, number = {34}, pages = {10496--10497}, posted-at = {2009-09-02 03:11:59}, priority = {2}, title = {Direct Carbon Detection in Paramagnetic Metalloproteins To Further Exploit Pseudocontact Shift Restraints}, url = {http://dx.doi.org/10.1021/ja047573m}, volume = {126}, year = {2004} }

TY - JOUR ID - citeulike:5705016 L3 - citeulike-article-id:5705016 N2 - PMID: 15327280 Direct detection heteronuclear NMR allows us to drastically reduce paramagnetic contributions to the line width as compared to 1H detection. As an example, a calcium binding protein (human oncomodulin), in which one of the calcium ions was selectively substituted with Tb3+, is used. Through a variety of 13C direct detection NMR experiments, resonances were detected as close as 5.5 A from the metal ion. Pseudocontact shifts measured through 13C direct detection experiments provide structural constraints in regions of the protein where 1H resonances are broadened beyond detection through Curie relaxation (up to 16 A from the paramagnetic center). IS - 34 JF - Journal of the American Chemical Society EP - 10497 TI - Direct Carbon Detection in Paramagnetic Metalloproteins To Further Exploit Pseudocontact Shift Restraints VL - 126 SP - 10496 KW - carbon_detection KW - nmr KW - pre AU - Babini, Elena AU - Bertini, Ivano AU - Capozzi, Francesco AU - Felli, Isabella AU - Lelli, Moreno AU - Luchinat, Claudio PY - 2004/09/01/ UR - http://dx.doi.org/10.1021/ja047573m ER -