Significantly improved resolution for noe correlations from valine and isoleucine (C(y)2) methyl groups in 15N, 13C- and 15N, 13C, 2H-labeled proteins

Catherine Zwahlen, Sébastien J F Vincent, Kevin H. Gardner, Lewis E. Kay

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

A new NMR experiment is described for recording NOEs from Val and Ile methyl groups in 15N, 13C-labeled or methyl-protonated, 15N, 13C, 2H-labeled proteins that offers far superior resolution than conventional 3D 13C-edited NOESY data sets. Resolution is achieved by recording both the C(β) and C(γ) (Val) or C(γ2) (Ile) chemical shifts as well as the chemical shift of the destination proton, and a strategy is introduced for refocusing homonuclear carbon couplings during the constant-time evolution of C(β) carbon magnetization. The utility of the method is demonstrated with applications on a 160- residue fully proton areal 15N, 13C-labeled, dNumb PTB domain- peptide complex and a methyl protonated, highly deuterated 15N, 13C-labeled complex of maltose binding protein and β-cyclodextrin (42 kDa).

Original languageEnglish (US)
Pages (from-to)4825-4831
Number of pages7
JournalJournal of the American Chemical Society
Volume120
Issue number19
DOIs
StatePublished - May 20 1998

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Isoleucine
Valine
Chemical shift
Protons
Carbon
Maltose-Binding Proteins
Proteins
Maltose
Cyclodextrins
Peptides
Magnetization
Nuclear magnetic resonance
Experiments
Carrier Proteins
Datasets
Protein Domains

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Significantly improved resolution for noe correlations from valine and isoleucine (C(y)2) methyl groups in 15N, 13C- and 15N, 13C, 2H-labeled proteins. / Zwahlen, Catherine; Vincent, Sébastien J F; Gardner, Kevin H.; Kay, Lewis E.

In: Journal of the American Chemical Society, Vol. 120, No. 19, 20.05.1998, p. 4825-4831.

Research output: Contribution to journalArticle

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abstract = "A new NMR experiment is described for recording NOEs from Val and Ile methyl groups in 15N, 13C-labeled or methyl-protonated, 15N, 13C, 2H-labeled proteins that offers far superior resolution than conventional 3D 13C-edited NOESY data sets. Resolution is achieved by recording both the C(β) and C(γ) (Val) or C(γ2) (Ile) chemical shifts as well as the chemical shift of the destination proton, and a strategy is introduced for refocusing homonuclear carbon couplings during the constant-time evolution of C(β) carbon magnetization. The utility of the method is demonstrated with applications on a 160- residue fully proton areal 15N, 13C-labeled, dNumb PTB domain- peptide complex and a methyl protonated, highly deuterated 15N, 13C-labeled complex of maltose binding protein and β-cyclodextrin (42 kDa).",
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N2 - A new NMR experiment is described for recording NOEs from Val and Ile methyl groups in 15N, 13C-labeled or methyl-protonated, 15N, 13C, 2H-labeled proteins that offers far superior resolution than conventional 3D 13C-edited NOESY data sets. Resolution is achieved by recording both the C(β) and C(γ) (Val) or C(γ2) (Ile) chemical shifts as well as the chemical shift of the destination proton, and a strategy is introduced for refocusing homonuclear carbon couplings during the constant-time evolution of C(β) carbon magnetization. The utility of the method is demonstrated with applications on a 160- residue fully proton areal 15N, 13C-labeled, dNumb PTB domain- peptide complex and a methyl protonated, highly deuterated 15N, 13C-labeled complex of maltose binding protein and β-cyclodextrin (42 kDa).

AB - A new NMR experiment is described for recording NOEs from Val and Ile methyl groups in 15N, 13C-labeled or methyl-protonated, 15N, 13C, 2H-labeled proteins that offers far superior resolution than conventional 3D 13C-edited NOESY data sets. Resolution is achieved by recording both the C(β) and C(γ) (Val) or C(γ2) (Ile) chemical shifts as well as the chemical shift of the destination proton, and a strategy is introduced for refocusing homonuclear carbon couplings during the constant-time evolution of C(β) carbon magnetization. The utility of the method is demonstrated with applications on a 160- residue fully proton areal 15N, 13C-labeled, dNumb PTB domain- peptide complex and a methyl protonated, highly deuterated 15N, 13C-labeled complex of maltose binding protein and β-cyclodextrin (42 kDa).

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