Literature DB >> 22911559

Assignment of the backbone carbonyl resonances in (15)N-labelled proteins with (13)C at natural abundance by a 2D triple-resonance correlation technique.

S M Kristensen1, M D Sørensen, J J Led.   

Abstract

A 2D NMR experiment for assignment of backbone carbon resonances in small and medium-sized (15)N-labelled proteins with (13)C at natural abundance is presented. The experiment is a two-dimensional variant of the HNCO triple-resonance experiment and is demonstrated by application to a 6 kDa protein at relatively low concentration (2 mM) and temperature (30°C). The experiment is particularly suitable for assignment of carbonyl resonances.

Entities:  

Year:  1995        PMID： 22911559     DOI： 10.1007/BF00182284

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


  9 in total

1.  Correlation of carbon-13 and nitrogen-15 chemical shifts in selectively and uniformly labeled proteins by heteronuclear two-dimensional NMR spectroscopy.

Authors:  W M Westler; B J Stockman; Y Hosoya; Y Miyake; M Kainosho; J L Markley
Journal:  J Am Chem Soc       Date:  1988-08-01       Impact factor: 15.419

2.  Modifications of older model nuclear magnetic resonance console for collection of multinuclear, multidimensional spectral data.

Authors:  E S Mooberry; F Abildgaard; J L Markley
Journal:  Methods Enzymol       Date:  1994       Impact factor: 1.600

Review 3.  Chemical shifts as a tool for structure determination.

Authors:  D S Wishart; B D Sykes
Journal:  Methods Enzymol       Date:  1994       Impact factor: 1.600

4.  A systematic approach towards the complete assignment of 13C resonances for horse ferrocytochrome c.

Authors:  Y Gao; J Boyd; R J Williams
Journal:  Eur J Biochem       Date:  1990-12-12

5.  Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.

Authors:  P E Hansen
Journal:  Biochemistry       Date:  1991-10-29       Impact factor: 3.162

6.  Concerted two-dimensional NMR approaches to hydrogen-1, carbon-13, and nitrogen-15 resonance assignments in proteins.

Authors:  B J Stockman; M D Reily; W M Westler; E L Ulrich; J L Markley
Journal:  Biochemistry       Date:  1989-01-10       Impact factor: 3.162

7.  Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone.

Authors:  F Abildgaard; A M Jørgensen; J J Led; T Christensen; E B Jensen; F Junker; H Dalbøge
Journal:  Biochemistry       Date:  1992-09-15       Impact factor: 3.162

8.  A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

Authors:  M Ikura; L E Kay; A Bax
Journal:  Biochemistry       Date:  1990-05-15       Impact factor: 3.162

9.  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
  9 in total
  1 in total

1.  A combined HNCA/HNCO experiment for 15N labeled proteins with 13C at natural abundance.

Authors:  Eriks Kupce; D R Muhandiram; Lewis E Kay
Journal:  J Biomol NMR       Date:  2003-10       Impact factor: 2.835
  1 in total

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