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Assignment of the aromatic 1H-NMR resonances of myotoxin a isolated from the venom of Crotalus viridis viridis.
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Assignment of the aromatic 1H-NMR resonances of myotoxin a isolated from the venom of Crotalus viridis viridis.

Author: JT Henderson; RA Nieman; AL Bieber
Edition/Format: Article Article : English
Publication:Biochimica et biophysica acta, 1987 Aug 5; 914(2): 152-61
Database:From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
Summary:
The 400 MHz 1H-NMR spectrum of myotoxin a from the venom of Crotalus viridis viridis is described. The identification of spin systems in the aromatic region corresponding to the six aromatic residues of myotoxin a was completed using both one- and two-dimensional NMR spectroscopy and the pH dependence of chemical shifts. Assignments of these spin systems to specific residues was possible for the singly occurring  Read more...
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Details

Document Type: Article
All Authors / Contributors: JT Henderson; RA Nieman; AL Bieber
ISSN:0006-3002
OCLC Number: 114978972
Language Note: English
Awards:

Abstract:

The 400 MHz 1H-NMR spectrum of myotoxin a from the venom of Crotalus viridis viridis is described. The identification of spin systems in the aromatic region corresponding to the six aromatic residues of myotoxin a was completed using both one- and two-dimensional NMR spectroscopy and the pH dependence of chemical shifts. Assignments of these spin systems to specific residues was possible for the singly occurring amino acids Tyr-1 and Phe-12. Resonances from Tyr-1, His-5 and His-10 were shifted significantly from their random coil values in a pH-dependent manner. These shift perturbations were deemed evidence of a helical arrangement of the amino terminal region which placed these residues in close proximity to each other.

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