Cross-Correlated Relaxation Enhanced 1H-13C NMR Spectroscopy of Methyl Groups in Very High Molecular Weight Proteins and Protein Complexes Export

@article{citeulike:2823494, abstract = {Abstract: A comparison of HSQC and HMQC pulse schemes for recording 1H-13C correlation maps of protonated methyl groups in highly deuterated proteins is presented. It is shown that HMQC correlation maps can be as much as a factor of 3 more sensitive than their HSQC counterparts and that the sensitivity gains result from a TROSY effect that involves cancellation of intra-methyl dipolar relaxation interactions. 1H-13C correlation spectra are recorded on U-[15N,2H], Ile1-[13C,1H] samples of (i) malate synthase G, a 723 residue protein, at 37 and 5 C, and of (ii) the protease ClpP, comprising 14 identical subunits, each with 193 residues (305 kDa), at 5 C. The high quality of HMQC spectra obtained in short measuring times strongly suggests that methyl groups will be useful probes of structure and dynamics in supramolecular complexes.}, address = {Contribution from the Protein Engineering Network Centers of Excellence and Departments of Medical Genetics, Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario, Canada M5S 1A8}, author = {Tugarinov, V. and Hwang, P. M. and Ollerenshaw, J. E. and Kay, L. E.}, citeulike-article-id = {2823494}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/ja030153x}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/ja030153x}, day = {27}, doi = {10.1021/ja030153x}, journal = {J. Am. Chem. Soc.}, keywords = {biggies, methyl, nmr-methods, relaxation, trosy}, month = {August}, number = {34}, pages = {10420--10428}, posted-at = {2008-05-22 18:42:19}, priority = {3}, title = {Cross-Correlated Relaxation Enhanced 1H-13C NMR Spectroscopy of Methyl Groups in Very High Molecular Weight Proteins and Protein Complexes}, url = {http://dx.doi.org/10.1021/ja030153x}, volume = {125}, year = {2003} }

TY - JOUR ID - citeulike:2823494 L3 - citeulike-article-id:2823494 N2 - Abstract: A comparison of HSQC and HMQC pulse schemes for recording 1H-13C correlation maps of protonated methyl groups in highly deuterated proteins is presented. It is shown that HMQC correlation maps can be as much as a factor of 3 more sensitive than their HSQC counterparts and that the sensitivity gains result from a TROSY effect that involves cancellation of intra-methyl dipolar relaxation interactions. 1H-13C correlation spectra are recorded on U-[15N,2H], Ile1-[13C,1H] samples of (i) malate synthase G, a 723 residue protein, at 37 and 5 C, and of (ii) the protease ClpP, comprising 14 identical subunits, each with 193 residues (305 kDa), at 5 C. The high quality of HMQC spectra obtained in short measuring times strongly suggests that methyl groups will be useful probes of structure and dynamics in supramolecular complexes. IS - 34 JF - J. Am. Chem. Soc. AD - Contribution from the Protein Engineering Network Centers of Excellence and Departments of Medical Genetics, Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario, Canada M5S 1A8 EP - 10428 TI - Cross-Correlated Relaxation Enhanced 1H-13C NMR Spectroscopy of Methyl Groups in Very High Molecular Weight Proteins and Protein Complexes VL - 125 SP - 10420 KW - biggies KW - methyl KW - nmr-methods KW - relaxation KW - trosy AU - Tugarinov, V AU - Hwang, PM AU - Ollerenshaw, JE AU - Kay, LE PY - 2003/08/27/ UR - http://dx.doi.org/10.1021/ja030153x ER -