Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 An (H)C(CO)NH-TOCSY pulse scheme for sequential assignment of protonated methyl groups in otherwise deuterated (15)N, (13)C-labeled proteins.

Literature DB >> 20686885

An (H)C(CO)NH-TOCSY pulse scheme for sequential assignment of protonated methyl groups in otherwise deuterated (15)N, (13)C-labeled proteins.

K H Gardner¹, R Konrat, M K Rosen, L E Kay.

Abstract

A biosynthetic strategy has recently been developed for the production of (15)N, (13)C, (2)H-labeled proteins using (1)H(3)C-pyruvate as the sole carbon source and D(2)O as the solvent. The methyl groups of Ala, Val, Leu and Ile (gamma2 only) remain highly protonated, while the remaining positions in the molecule are largely deuterated. An (H)C(CO)NH-TOCSY experiment is presented for the sequential assignment of the protonated methyl groups. A high-sensitivity spectrum is recorded on a (15)N, (13)C, (2)H, (1)H(3)C-labeled SH2 domain at 3 degrees C (correlation time 18.8 ns), demonstrating the utility of the method for proteins in the 30-40 kDa molecular weight range.

Entities: Chemical Gene

Year: 1996 PMID： 20686885 DOI： 10.1007/BF00410333

Source DB: PubMed Journal: J Biomol NMR ISSN： 0925-2738 Impact factor: 2.835

9 in total

1. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death.

Authors: S W Muchmore; M Sattler; H Liang; R P Meadows; J E Harlan; H S Yoon; D Nettesheim; B S Chang; C B Thompson; S L Wong; S L Ng; S W Fesik
Journal: Nature Date: 1996-05-23 Impact factor: 49.962

2. Assignment of aliphatic side-chain 1HN/15N resonances in perdeuterated proteins.

Authors: B T Farmer; R A Venters
Journal: J Biomol NMR Date: 1996-01 Impact factor: 2.835

3. The use of heteronuclear cross-polarization for backbone assignment of (2)H-, (15)N- and (13)C-labeled proteins: A pulse scheme for triple-resonance 4D correlation of sequential amide protons and (15)N.

Authors: M Shirakawa; M Wälchli; M Shimizu; Y Kyogoku
Journal: J Biomol NMR Date: 1995-04 Impact factor: 2.835

4. Structure and ligand recognition of the phosphotyrosine binding domain of Shc.

Authors: M M Zhou; K S Ravichandran; E F Olejniczak; A M Petros; R P Meadows; M Sattler; J E Harlan; W S Wade; S J Burakoff; S W Fesik
Journal: Nature Date: 1995-12-07 Impact factor: 49.962

5. Effect of deuteration on the amide proton relaxation rates in proteins. Heteronuclear NMR experiments on villin 14T.

Authors: M A Markus; K T Dayie; P Matsudaira; G Wagner
Journal: J Magn Reson B Date: 1994-10

6. Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments.

Authors: T M Logan; E T Olejniczak; R X Xu; S W Fesik
Journal: FEBS Lett Date: 1992-12-21 Impact factor: 4.124

7. Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.

Authors: S Grzesiek; A Bax
Journal: J Biomol NMR Date: 1993-03 Impact factor: 2.835

8. A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments.

Authors: T M Logan; E T Olejniczak; R X Xu; S W Fesik
Journal: J Biomol NMR Date: 1993-03 Impact factor: 2.835

9. Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.

Authors: N A Farrow; R Muhandiram; A U Singer; S M Pascal; C M Kay; G Gish; S E Shoelson; T Pawson; J D Forman-Kay; L E Kay
Journal: Biochemistry Date: 1994-05-17 Impact factor: 3.162

9 in total

31 in total

1. Efficient side-chain and backbone assignment in large proteins: application to tGCN5.

Authors: Y Lin; G Wagner
Journal: J Biomol NMR Date: 1999-11 Impact factor: 2.835

2. Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy.

Authors: Vincenzo Venditti; Nicolas L Fawzi; G Marius Clore
Journal: J Biomol NMR Date: 2011-09-04 Impact factor: 2.835

10. Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form.

Authors: S Uhrínová; D Uhrín; H Denton; M Smith; L Sawyer; P N Barlow
Journal: J Biomol NMR Date: 1998-07 Impact factor: 2.835

An (H)C(CO)NH-TOCSY pulse scheme for sequential assignment of protonated methyl groups in otherwise deuterated (15)N, (13)C-labeled proteins.

1. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death.

2. Assignment of aliphatic side-chain 1HN/15N resonances in perdeuterated proteins.

3. The use of heteronuclear cross-polarization for backbone assignment of (2)H-, (15)N- and (13)C-labeled proteins: A pulse scheme for triple-resonance 4D correlation of sequential amide protons and (15)N.

4. Structure and ligand recognition of the phosphotyrosine binding domain of Shc.

5. Effect of deuteration on the amide proton relaxation rates in proteins. Heteronuclear NMR experiments on villin 14T.

6. Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments.

7. Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.

8. A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments.

9. Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.

1. Efficient side-chain and backbone assignment in large proteins: application to tGCN5.

2. Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy.

3. Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints.

4. MONTE: An automated Monte Carlo based approach to nuclear magnetic resonance assignment of proteins.

5. Data requirements for reliable chemical shift assignments in deuterated proteins.

6. Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains.

7. Mars -- robust automatic backbone assignment of proteins.

8. High resolution methyl selective ¹³C-NMR of proteins in solution and solid state.

9. Structure and dynamics of copper-free SOD: The protein before binding copper.

10. Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form.