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Tetanus toxin conformation

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Summary

The circular dichroic spectrum of highly purified tetanus toxin has been determined between 200–310 nm. A comparison of the ellipticity between 207–243 nm and of the rotational strengths of the major resolved bands between 200–250 nm with the corresponding values from proteins of known conformation indicates that tetanus toxin contains about 20% α-helix and 23% β-structure. Above 250 nm the resolved spectrum showed contributions from tryptophanyl, tyrosyl, and phenylalanyl groups. The rotational strengths of the major near ultraviolet circular dichroic bands were significantly higher in the toxin than in low molecular weight peptides containing aromatic residues. This indicates that tetanus toxin has a stable tertiary structure.

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Authors and Affiliations

  1. Departments of Microbiology and Biochemistry, Vanderbilt University, 37232, Nashville, Tennessee, USA

    John P. Robinson, Leslie A. Holladay, John B. Picklesimer & David Puett

Authors
  1. John P. Robinson
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  2. Leslie A. Holladay
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  3. John B. Picklesimer
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  4. David Puett
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Additional information

Andrew W. Mellon Foundation Teacher-Scholar Awardee.

Camille and Henry Dreyfus Foundation Teacher-Scholar Awardee.

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Robinson, J.P., Holladay, L.A., Picklesimer, J.B. et al. Tetanus toxin conformation. Mol Cell Biochem 5, 147–151 (1974). https://doi.org/10.1007/BF01731377

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  • DOI: https://doi.org/10.1007/BF01731377

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