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Sequence-specific h-1-NMR assignments and determination of the secondary structure in aqueous-solution of the cardiotoxin-ctxiia and cardiotoxin-ctxiib from naja-mossambica-mossambica

Academic Article
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Overview

authors

  • Otting, G.
  • Steinmetz, W. E.
  • Bougis, P. E.
  • Rochat, H.
  • Wuthrich, Kurt

publication date

  • November 1987

journal

  • European Journal of Biochemistry  Journal

abstract

  • Sequence-specific assignments of the 1H-nuclear magnetic resonance (NMR) spectra of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica were obtained using two-dimensional NMR experiments at 500 MHz and the independently determined amino acid sequences. Assignments were obtained from data at 25 degrees C and 45 degrees C for all but one backbone proton of the 60 residues in each protein. Complete or partial assignments are also reported for the side-chain protons. These assignments supercede those published previously for the toxin preparation VII2 [Hosur, R. V., Wider, G. & Wüthrich K. (1983) Eur. J. Biochem. 130, 497-508]. The 1H/2H-exchange kinetics were measured in 2H2O at 20 degrees C for the amide protons and the N-terminal amino group. These and additional NMR data enabled the determination of the secondary structure in aqueous solution, which is virtually identical in CTXIIa and CTXIIb. Both proteins contain a short double-stranded antiparallel beta-sheet comprising the residues 2-4 and 11-13, and a triple-stranded antiparallel beta-sheet consisting of the residues 20-26, 35-39, and 49-55. The two peripheral strands of the triple-stranded beta-structure were found to be connected by a right-handed cross-over, and the locations of several tight turns were also identified.

subject areas

  • Amino Acid Sequence
  • Amino Acids
  • Energy Transfer
  • Heart
  • Magnetic Resonance Spectroscopy
  • Protein Conformation
  • Proteins
  • Protons
  • Snake Venoms
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Identity

International Standard Serial Number (ISSN)

  • 0014-2956

Digital Object Identifier (DOI)

  • 10.1111/j.1432-1033.1987.tb13460.x

PubMed ID

  • 2822421
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Additional Document Info

start page

  • 609

end page

  • 620

volume

  • 168

issue

  • 3

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