Literature DB >> 9740741

PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic proteins.

A Bondon1, C Mouro.   

Abstract

A new method for NMR spectra acquisition of paramagnetic proteins is described, based on the simple use of homonuclear broadband decoupling of the diamagnetic region. Several advantages are associated with this method which was applied to one-dimensional spectra, to 1D NOE-difference spectroscopy, and to 2D NOESY. The main advantage is a very flat baseline obtained using the PASE (paramagnetic signals enhancement) method. Furthermore, the bulky region of the diamagnetic protons being suppressed, clean NOE-difference spectra can be acquired as well as improved 2D NOESY maps. Applications on 1D 1H spectrum of bovine liver catalase (MW 230,000), and 1D and 2D on the high-spin form of the myoglobin, used as a model protein, are presented. Copyright 1998 Academic Press.

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Year:  1998        PMID: 9740741     DOI: 10.1006/jmre.1998.1523

Source DB:  PubMed          Journal:  J Magn Reson        ISSN: 1090-7807            Impact factor:   2.229


  5 in total

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Journal:  J Biol Chem       Date:  2012-06-14       Impact factor: 5.157

2.  Ligation and Reactivity of Methionine-Oxidized Cytochrome c.

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Journal:  Inorg Chem       Date:  2018-04-30       Impact factor: 5.165

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Authors:  Gregory Da Costa; Soizic Chevance; Elisabeth Le Rumeur; Arnaud Bondon
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4.  Electron spin density on the axial His ligand of high-spin and low-spin nitrophorin 2 probed by heteronuclear NMR spectroscopy.

Authors:  Luciano A Abriata; María-Eugenia Zaballa; Robert E Berry; Fei Yang; Hongjun Zhang; F Ann Walker; Alejandro J Vila
Journal:  Inorg Chem       Date:  2013-01-17       Impact factor: 5.165

5.  Outer-sphere contributions to the electronic structure of type zero copper proteins.

Authors:  Kyle M Lancaster; María-Eugenia Zaballa; Stephen Sproules; Mahesh Sundararajan; Serena DeBeer; John H Richards; Alejandro J Vila; Frank Neese; Harry B Gray
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  5 in total

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