Allan L. BIEBER

University of New South Wales, Kensington, New South Wales, Australia

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Publications (2)3.58 Total impact

  • [Show abstract] [Hide abstract]
    ABSTRACT: Sequence-specific resonance assignments are reported for the 500-MHz 1H-NMR spectrum of the 55-residue neurotoxin B-IV, isolated from the heteronemertine worm Cerebratulus lacteus. A range of two-dimensional homonuclear correlated and NOE spectra was used in making these assignments, which include NH, CαH and CβH resonances, as well as most resonances from longer-chain spin systems, with the exception of the ten Lys residues, where spectral overlap prevented complete, unambiguous assignments. The secondary structure of B-IV was identified from the pattern of sequential (i, i+ 1) and medium range (i, i+ 2/3/4) NOE connectivities and the location of slowly exchanging backbone amide protons. Two helices are present, incorporating residues 13–26 and 33–49, and the C-terminal five residues form a helix-like structure. A type-I reverse turn, involving residues 28–31 is present in a small loop linking the two major helices, and the N-terminus appears to be unordered at 27°C, although it may adopt a more ordered conformation at lower temperatures. These elements of secondary structure, together with the four disulfide bonds in the protein, provide sufficient information to define the global fold of the molecule in solution. The pH and temperature dependence of the toxin have been investigated by 1H-NMR and the pKa values of several ionisable sidechains determined.
    European Journal of Biochemistry. 03/2005; 210(1):231 - 240.
  • P E Hansen, W R Kem, A L Bieber, R S Norton
    [Show abstract] [Hide abstract]
    ABSTRACT: Sequence-specific resonance assignments are reported for the 500-MHz 1H-NMR spectrum of the 55-residue neurotoxin B-IV, isolated from the heteronemertine worm Cerebratulus lacteus. A range of two-dimensional homonuclear correlated and NOE spectra was used in making these assignments, which include NH, C alpha H and C beta H resonances, as well as most resonances from longer-chain spin systems, with the exception of the ten Lys residues, where spectral overlap prevented complete, unambiguous assignments. The secondary structure of B-IV was identified from the pattern of sequential (i, i + 1) and medium range (i, i + 2/3/4) NOE connectivities and the location of slowly exchanging backbone amide protons. Two helices are present, incorporating residues 13-26 and 33-49, and the C-terminal five residues form a helix-like structure. A type-I reverse turn, involving residues 28-31 is present in a small loop linking the two major helices, and the N-terminus appears to be unordered at 27 degrees C, although it may adopt a more ordered conformation at lower temperatures. These elements of secondary structure, together with the four disulfide bonds in the protein, provide sufficient information to define the global fold of the molecule in solution. The pH and temperature dependence of the toxin have been investigated by 1H-NMR and the pKa values of several ionisable sidechains determined.
    European Journal of Biochemistry 12/1992; 210(1):231-40. · 3.58 Impact Factor

Publication Stats

1 Citation
3.58 Total Impact Points

Institutions

  • 2005
    • University of New South Wales
      Kensington, New South Wales, Australia