Significantly Improved Resolution for NOE Correlations from Valine and Isoleucine (C2) Methyl Groups in 1
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- 作者：Catherine Zwahlen ; Sé ; bastien J. F. Vincent ; Kevin H. Gardner ; and Lewis E. Kay
- 刊名：Journal of the American Chemical Society
- 出版年：1998
- 出版时间：May 20, 1998
- 年：1998
- 卷：120
- 期：19
- 页码：4825 - 4831
- 全文大小：170K
- 年卷期：v.120,no.19(May 20, 1998)
- ISSN：1520-5126
文摘
A new NMR experiment is described for recording NOEs from Val andIle methyl groups in 15N,13C-labeled or methyl-protonated,15N,13C,2H-labeled proteins thatoffers far superior resolution than conventional3D 13C-edited NOESY data sets. Resolution is achievedby recording both the C
and C
(Val) orC2 (Ile)chemical shifts as well as the chemical shift of the destinationproton, and a strategy is introduced for refocusinghomonuclear carbon couplings during the constant-time evolution ofC carbon magnetization. The utility ofthe method is demonstrated with applications on a 160-residue fullyprotonated 15N,13C-labeled, dNumbPTBdomain-peptide complex and a methyl protonated, highly deuterated15N,13C-labeled complex of maltosebinding protein and -cyclodextrin (42 kDa).
and C (Val) orC2 (Ile)chemical shifts as well as the chemical shift of the destinationproton, and a strategy is introduced for refocusinghomonuclear carbon couplings during the constant-time evolution ofC carbon magnetization. The utility ofthe method is demonstrated with applications on a 160-residue fullyprotonated 15N,13C-labeled, dNumbPTBdomain-peptide complex and a methyl protonated, highly deuterated15N,13C-labeled complex of maltosebinding protein and -cyclodextrin (42 kDa).