NMR analysis and sequence of toxin II from the sea anemone Radianthus paumotensis.

Toxin II from Radianthus paumotensis (RpII) has been investigated by high-resolution NMR and chemical sequencing methods. Resonance assignments have been obtained for this protein by the sequential approach. NMR assignments could not be made consistent with the previously reported primary sequence for this protein, and chemical methods have been used to determine a sequence with which the NMR data are consistent. Analysis of the 2D NOE spectra shows that the protein secondary structure is comprised of two sequences of beta-sheet, probably joined into a distorted continuous sheet, connected by turns and extended loops, without any regular alpha-helical segments. The residues previously implicated in activity in this class of proteins, D8 and R13, occur in a loop region.

[1]  R. Norton,et al.  Secondary structure in sea anemone polypeptides: a proton nuclear magnetic resonance study , 1986 .

[2]  R. Norton,et al.  Specific assignment of resonances in the 1H‐nmr spectrum of the polypeptide toxin I from Anemonia sulcata , 1986, Biopolymers.

[3]  G. Drobny,et al.  1H NMR studies of lambda cro repressor. 1. Selective optimization of two-dimensional relayed coherence transfer spectroscopy. , 1985, Biochemistry.

[4]  D. Wemmer,et al.  Complete assignment of the imino protons of Escherichia coli valine transfer RNA: two-dimensional NMR studies in water. , 1985, Biochemistry.

[5]  A. Tsugita,et al.  Purification, sequence, and pharmacological properties of sea anemone toxins from Radianthus paumotensis. A new class of sea anemone toxins acting on the sodium channel. , 1985, Biochemistry.

[6]  Timothy F. Havel,et al.  An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution. , 1985, Journal of molecular biology.

[7]  Timothy F. Havel,et al.  Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry. , 1985, Journal of molecular biology.

[8]  W F van Gunsteren,et al.  A protein structure from nuclear magnetic resonance data. lac repressor headpiece. , 1985, Journal of molecular biology.

[9]  A. Bax,et al.  Optimization of two-dimensional homonuclear relayed coherence transfer NMR spectroscopy , 1985 .

[10]  K Wüthrich,et al.  Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. , 1984, Journal of molecular biology.

[11]  K. Wüthrich,et al.  Two-dimensional 1H NMR of two chemically modified analogs of the basic pancreatic trypsin inhibitor. Sequence-specific resonance assignments and sequence location of conformation changes relative to the native protein. , 1984, European journal of biochemistry.

[12]  R. Norton,et al.  1H nuclear magnetic resonance spectroscopic study of the polypeptide toxin I from Anemonia sulcata , 1984 .

[13]  Kurt Wüthrich,et al.  Homonuclear two-dimensional 1H NMR of proteins. Experimental procedures , 1984 .

[14]  A. Maelicke,et al.  The sites of neurotoxicity in alpha-cobratoxin. , 1983, The Journal of biological chemistry.

[15]  D. Wemmer,et al.  Structure of apamin in solution: a two-dimensional nuclear magnetic resonance study. , 1983, Biochemistry.

[16]  K Wüthrich,et al.  Sequential individual resonance assignments in the 1H‐NMR spectra of polypeptides and proteins , 1983, Biopolymers.

[17]  D. States,et al.  A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants☆ , 1982 .

[18]  G. Bodenhausen,et al.  Exploring nuclear spin systems by relayed magnetization transfer , 1982 .

[19]  K Wüthrich,et al.  Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations. , 1982, Journal of molecular biology.

[20]  K Wüthrich,et al.  Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance. , 1982, Journal of molecular biology.

[21]  M. Lazdunski,et al.  Structure-function relationships of sea anemone toxin II from Anemonia sulcata. , 1981, The Journal of biological chemistry.

[22]  R. Norton,et al.  Natural abundance carbon-13 nuclear magnetic resonance study of anthopleurin-A, a cardiac stimulant from the sea anemone Anthopleura xanthogrammica. , 1979, The Journal of biological chemistry.

[23]  A. Tu,et al.  Conformational studies of peptide heart stimulant anthopleurin A. Laser Raman, circular dichroism, fluorescence spectral studies, and Chou-Fasman calculations. , 1979, The Journal of biological chemistry.

[24]  A. Tu,et al.  Structural properties of toxin II of sea anemone (Anemone sulcata) determined by laser raman spectroscopy , 1976, FEBS letters.

[25]  E. Haber,et al.  The application of 0.1 M quadrol to the microsequence of proteins and the sequence of tryptic peptides. , 1975, Biochemistry.

[26]  P. Edman,et al.  A protein sequenator. , 1967, European journal of biochemistry.

[27]  J. M. Minor,et al.  Simultaneous selectivity optimization of mobile and stationary phases in reversed-phased liquid chromatography for isocratic separations of phenylthiohydantoin amino acid derivatives , 1985 .

[28]  B. Reid,et al.  High Resolution NMR Studies of Nucleic Acids and Proteins , 1985 .

[29]  D. G. Bishop,et al.  Interaction of the polypeptide cardiac stimulant anthopleurin-A with H+, Ca2+, and membrane lipids. , 1982, Archives of Biochemistry and Biophysics.

[30]  G. Wunderer.  Die Disulfidbrücken von Toxin II aus Anemonia sulcata , 1978 .