Related ArticlesStereospecific assignments of the leucine methyl resonances in the 1H NMR spectrum of Lactobacillus casei dihydrofolate reductase.
FEBS Lett. 1993 Mar 1;318(2):177-80
Authors: Ostler G, Soteriou A, Moody CM, Khan JA, Birdsall B, Carr MD, Young DW, Feeney J
A general method is described for the stereospecific assignment of methyl resonances in protein NMR spectra based on selective deuteration procedures. A selectively deuterated dihydrofolate reductase from L. casei was prepared by incorporating stereoselectively deuterated L-leucine, (2S,4R)[5,5,5-2H3]leucine. By comparing the COSY spectra of the dihydrofolate reductase-methotrexate complexes formed using deuterated and non-deuterated enzyme the stereospecific assignments for resonances of all 13 leucine residues were obtained by noting the absence of cross-peaks in spectra from the deuterated proteins.
A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins
A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins
Abstract A new method for stereospecific assignment of prochiral methyl groups in proteins is presented in which protein samples are produced using U-glucose and subsaturating amounts of 2-methyl-acetolactate. The resulting non-uniform labeling pattern allows proR and proS methyl groups to be easily distinguished by their different phases in a constant-time two-dimensional 1H-13C correlation spectra. Protein samples are conveniently prepared using the same media composition as the...
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High-resolution methyl edited GFT NMR experiments for protein resonance assignments a
High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination
Abstract Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile, Leu, Met, Thr and Val) there is a significant overlap of 13C and 1H chemical shifts. Such overlap can be resolved using the recently proposed (3,2)D HCCH-COSY, a G-matrix Fourier transform (GFT) NMR based experiment, which facilitates editing...
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[NMR paper] Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT
Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR.
Related Articles Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR.
Biochemistry. 1993 Dec 7;32(48):13071-80
Authors: Abeygunawardana C, Weber DJ, Frick DN, Bessman MJ, Mildvan AS
The MutT protein, a 129-residue enzyme from Escherichia coli which prevents A.T-->C.G mutations, catalyzes the hydrolysis of nucleoside triphosphates (NTP)...
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[NMR paper] Complete assignments of magnetic resonances of ribonuclease H from Escherichia coli b
Complete assignments of magnetic resonances of ribonuclease H from Escherichia coli by double- and triple-resonance 2D and 3D NMR spectroscopies.
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Biochemistry. 1993 Jun 1;32(21):5656-69
Authors: Yamazaki T, Yoshida M, Nagayama K
Assignments of 1H, 15N, and 13C magnetic resonances for ribonuclease H from Escherichia coli have been completed using double- and triple-resonance 2D and 3D...
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[NMR paper] Assignments of backbone 1H, 13C, and 15N resonances and secondary structure of ribonu
Assignments of backbone 1H, 13C, and 15N resonances and secondary structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Assignments of backbone 1H, 13C, and 15N resonances and secondary structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1991 Jun 18;30(24):6036-47
Authors: Yamazaki T, Yoshida M, Kanaya S, Nakamura H, Nagayama K
The assignments of individual magnetic resonances of backbone nuclei of a larger...
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[NMR paper] The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei
The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei dihydrofolate reductase and the origins of their chemical shifts.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei dihydrofolate reductase and the origins of their chemical shifts.
Eur J Biochem. 1990 Aug 17;191(3):659-68
Authors: Birdsall B, Arnold JR, Jimenez-Barbero J,...
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Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in t
Abstract HNCO/HNCACO type correlation experiments are an alternative for assignment of backbone resonances in extensively deuterated proteins in the solid-state, given the fact that line widths on the order of 14â??17 Hz are achieved in the carbonyl dimension without the need of high power decoupling. The achieved resolution demonstrates that MAS solid-state NMR on extensively deuterated proteins is able to compete with solution-state NMR spectroscopy if proteins are investigated with correlation times Ï? c that exceed 25 ns.
Content Type Journal Article
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Stereospecific assignments of the leucine methyl resonances in the 1H NMR spectrum of
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