Literature DB >> 9740750

The new active-coupling-pattern tilting experiment for an efficient and accurate determination of homonuclear coupling constants

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Abstract

A new constant-time COSY experiment which allows an efficient determination of accurate homonuclear coupling constant values is presented. Characteristic features include an improved scheme for homonuclear active-coupling-pattern tilting (ACT) and an arbitrarily scaled shift and coupling information (ASSCI) design of the F1 domain. As a result, simple and easy to interpret tilted cross-peak patterns, even for two-spin systems, are obtained with good sensitivity. The relative spacing of chemical-shift differences and coupling splittings is largely under experimental control. The effectiveness of the spectral region selective variant of the new sequence is demonstrated by a determination of the 3JHN, Halpha couplings in a peptide sample. The multiplet-selective variant is shown to produce good results with a terpene. The superiority of the new ACT scheme is additionally demonstrated by an ACT-J spectrum of the peptide. Copyright 1998 Academic Press.

Entities:  

Year:  1998        PMID: 9740750     DOI: 10.1006/jmre.1998.1479

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


  1 in total

1.  NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.

Authors:  T Cierpicki; J Bania; J Otlewski
Journal:  Protein Sci       Date:  2000-05       Impact factor: 6.725

  1 in total

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