@article {2525,
	title = {Detection and assignment of phosphoserine and phosphothreonine residues by C-13-P-31 spin-echo difference NMR spectroscopy},
	journal = {Journal of Biomolecular Nmr},
	volume = {43},
	number = {1},
	year = {2009},
	note = {ISI Document Delivery No.: 379QKTimes Cited: 0Cited Reference Count: 31McIntosh, Lawrence P. Kang, Hyun-Seo Okon, Mark Nelson, Mary L. Graves, Barbara J. Brutscher, Bernhard},
	month = {Jan},
	pages = {31-37},
	type = {Article},
	abstract = {A simple NMR method is presented for the identification and assignment of phosphorylated serine and threonine residues in C-13- or C-13/N-15-labeled proteins. By exploiting modest (similar to 5 Hz) 2- and 3-bond C-13-P-31 scalar couplings, the aliphatic H-1-C-13 signals from phosphoserines and phosphothreonines can be detected selectively in a P-31 spin-echo difference constant time H-1-C-13 HSQC spectrum. Inclusion of the same P-31 spin-echo element within the C-13 frequency editing period of an intraHNCA or HN(CO)CA experiment allows identification of the amide H-1(N) and N-15 signals of residues (i) for which C-13(alpha)(i) or C-13(alpha)(i - 1), respectively, are coupled to a phosphate. Furthermore, P-31 resonance assignments can be obtained by applying selective low power cw P-31 decoupling during the spin-echo period. The approach is demonstrated using a PNT domain containing fragment of the transcription factor Ets-1, phosphorylated in vitro at Thr38 and Ser41 with the MAP kinase ERK2.},
	keywords = {ASSIGNMENT, CENTER-DOT-OP, CONSTANT-TIME, Ets-1, MAP kinase, NUCLEIC-ACIDS, OP HYDROGEN-BONDS, P-31-C-13 scalar coupling, Phosphoprotein, PHOSPHORYLATION, POINTED DOMAIN, PROTEIN, QUANTITATIVE J-CORRELATION, RESONANCE, SCALAR COUPLINGS, TRANSCRIPTION FACTOR},
	isbn = {0925-2738},
	url = {<Go to ISI>://000261411100004},
	author = {McIntosh, L. P. and Kang, H. S. and Okon, M. and Nelson, M. L. and Graves, B. J. and Brutscher, B.}
}
