Literature DB >> 7703702

HCCH-TOCSY spectroscopy of 13C-labeled proteins in H2O using heteronuclear cross-polarization and pulsed-field gradients.

H Wang1, E R Zuiderweg.   

Abstract

A pulsed-field gradient-enhanced, heteronuclear cross-polarization-driven, 3D HCCH-TOCSY experiment is described, which in a single scan can achieve nearly ideal solvent suppression for protein samples in H2O solution. The 3D experiment can be transformed without additional pre- or post-processing, thus leaving solute resonances at the solvent resonance position undisturbed and easily identifiable. As the gradients are used in combination with a 13C z-filter, only minimal relaxation losses are encountered as compared to non-gradient versions.

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Year:  1995        PMID： 7703702     DOI： 10.1007/bf00208812

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


  6 in total

1.  A complete set of novel 2D correlation NMR experiments based on heteronuclear J-cross polarization.

Authors:  Teodor Parella
Journal:  J Biomol NMR       Date:  2004-05       Impact factor: 2.835

2.  Band-selective hetero- and homonuclear cross-polarization using trains of shaped pulses.

Authors:  E R Zuiderweg; L Zeng; B Brutscher; R C Morshauser
Journal:  J Biomol NMR       Date:  1996-09       Impact factor: 2.835

3.  Improved NMR experiments with ¹³C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.

Authors:  Helena Kovacs; Alvar Gossert
Journal:  J Biomol NMR       Date:  2014-01-04       Impact factor: 2.835

4.  Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α3DIV, that Sequesters Toxic Heavy Metals.

Authors:  Jefferson S Plegaria; Stephen P Dzul; Erik R P Zuiderweg; Timothy L Stemmler; Vincent L Pecoraro
Journal:  Biochemistry       Date:  2015-04-29       Impact factor: 3.162

5.  Novel multi-dimensional heteronuclear NMR techniques for the study of 13C-O-acetylated oligosaccharides: expanding the dimensions for carbohydrate structures.

Authors:  D N Jones; B Bendiak
Journal:  J Biomol NMR       Date:  1999-10       Impact factor: 2.835

6.  Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase/protease I: a member of a new subclass of lipolytic enzymes.

Authors:  T H Lin; C Chen; R F Huang; Y L Lee; J F Shaw; T H Huang
Journal:  J Biomol NMR       Date:  1998-05       Impact factor: 2.835
  6 in total

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