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Literature DB >> 1283353

A 4D HCCH-TOCSY experiment for assigning the side chain 1H and 13C resonances of proteins.

Abstract

A 4D HCCH-TOCSY experiment is described for correlating and assigning the 1H and 13C resonances of protein amino acid side chains that has several advantages over 3D versions of the experiment. In many cases, both the 1H and 13C chemical shifts can be obtained in the 4D experiment from a simple inspection of the 13C(omega 3), 1H(omega 4) planes extracted at the 1H alpha(omega 1)/13C alpha(omega 2) chemical shifts. Together with the 3D and 4D triple resonance experiments, this allows sequence-specific assignments to be obtained. In addition, the increased resolution of the 4D experiment compared to its 3D counterpart allows automation of resonance assignments.

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Year: 1992 PMID： 1283353 DOI： 10.1007/BF02192854

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

12 in total

1. Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.

Authors: G M Clore; A Bax; P C Driscoll; P T Wingfield; A M Gronenborn
Journal: Biochemistry Date: 1990-09-04 Impact factor: 3.162

2. An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins.

Authors: A Bax; M Ikura
Journal: J Biomol NMR Date: 1991-05 Impact factor: 2.835

3. Assignment of the aliphatic 1H and 13C resonances of the Bacillus subtilis glucose permease IIA domain using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.

Authors: W J Fairbrother; A G Palmer; M Rance; J Reizer; M H Saier; P E Wright
Journal: Biochemistry Date: 1992-05-12 Impact factor: 3.162

4. FR-900520 and FR-900523, novel immunosuppressants isolated from a Streptomyces. II. Fermentation, isolation and physico-chemical and biological characteristics.

Authors: H Hatanaka; T Kino; S Miyata; N Inamura; A Kuroda; T Goto; H Tanaka; M Okuhara
Journal: J Antibiot (Tokyo) Date: 1988-11 Impact factor: 2.649

5. Protein carbon-13 spin systems by a single two-dimensional nuclear magnetic resonance experiment.

Authors: B H Oh; W M Westler; P Darba; J L Markley
Journal: Science Date: 1988-05-13 Impact factor: 47.728

6. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin.

Authors: J J Siekierka; S H Hung; M Poe; C S Lin; N H Sigal
Journal: Nature Date: 1989-10-26 Impact factor: 49.962

7. A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase.

Authors: M W Harding; A Galat; D E Uehling; S L Schreiber
Journal: Nature Date: 1989-10-26 Impact factor: 49.962

8. 1H, 15N, 13C, and 13CO assignments of human interleukin-4 using three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy.

Authors: R Powers; D S Garrett; C J March; E A Frieden; A M Gronenborn; G M Clore
Journal: Biochemistry Date: 1992-05-05 Impact factor: 3.162

9. Solution studies of staphylococcal nuclease H124L. 2. 1H, 13C, and 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3',5'-bisphosphate-calcium ternary complex.

Authors: J F Wang; A P Hinck; S N Loh; D M LeMaster; J L Markley
Journal: Biochemistry Date: 1992-01-28 Impact factor: 3.162

10. Toward the complete assignment of the carbon nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitor.

Authors: G Wagner; D Brühwiler
Journal: Biochemistry Date: 1986-10-07 Impact factor: 3.162

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Journal: Biophys J Date: 2009-04-22 Impact factor: 4.033

3. 3D HCCH-COSY-TOCSY experiment for the assignment of ribose and amino acid side chains in 13C labeled RNA and protein.

Authors: W Hu; L T Kakalis; L Jiang; F Jiang; X Ye; A Majumdar
Journal: J Biomol NMR Date: 1998-11 Impact factor: 2.835

4. A computer-based protocol for semiautomated assignments and 3D structure determination of proteins.

Authors: R P Meadows; E T Olejniczak; S W Fesik
Journal: J Biomol NMR Date: 1994-01 Impact factor: 2.835

5. The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.

Authors: E Ab; G Schuurman-Wolters; J Reizer; M H Saier; K Dijkstra; R M Scheek; G T Robillard
Journal: Protein Sci Date: 1997-02 Impact factor: 6.725

6. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins.

Authors: Wade M Borcherds; Gary W Daughdrill
Journal: Methods Enzymol Date: 2018-10-22 Impact factor: 1.600

7. Comparison of fragments comprising the first two helices of the human Y4 and the yeast Ste2p G-protein-coupled receptors.

Authors: Xuan Shao; Chao Zou; Fred Naider; Oliver Zerbe
Journal: Biophys J Date: 2012-08-22 Impact factor: 4.033