J-modulated TROSY experiment extends the limits of homonuclear coupling measurements for larger proteins.
This paper describes the use of a TROSY experimental scheme and its variant extended with a scaled J-modulation spin-echo sequence for accurate and sensitive measurement of homonuclear 3J(H(N)H(alpha)) coupling constants in larger proteins with uniform 15N labeling. Exclusive selection of the most slowly relaxing component of a 15N-1H multiplet by the TROSY approach leads to substantial improvement in resolution; this is a prerequisite for accurate measurement of couplings from the 1H multiplets directly along the 1H frequency dimension or from the J-scaled doublets along the 15N frequency dimension.
Kövér
K E
KE
Department of Inorganic and Analytical Chemistry, University of Debrecen, Hungary. kover@tigris.klte.hu
Batta
G
G
D000465:Algorithms; D009682:Magnetic Resonance Spectroscopy; D009587:Nitrogen Isotopes; D011506:Proteins / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry; D014452:Ubiquitins / Q000737:chemistry
D009587:Nitrogen Isotopes; D011506:Proteins; D014452:Ubiquitins; D012260:Ribonucleases