Letter | Published:

Sense of the Helix in Poly-L-tyrosine

Nature volume 193, pages 681682 (17 February 1962) | Download Citation

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Abstract

THE anomalous rotatory dispersion curves for many synthetic poly-α-amino-acids in the helical conformation have been adequately interpreted by the equation proposed by Moffitt1. The constant, b0, in this equation has been used as a measure of helix content in polypeptides and proteins2. The sign of b0 has been taken to signify the sense of the helix1,3–6. A value of approximately − 630 has been found for the helical conformation of poly-L-glutamic acid1a, poly-γ-benzyl-L-glutamate1,4 and for poly-L-alanine7; the latter has been shown to exist as a right-handed helix8. The first reported positive b0 value was that found for poly-L-tyrosine7, and it was suggested that the unusual sign of b0 is a consequence of a strong chromophoric group near the β-carbon. Other positive b0 values have since been reported for poly-β-benzyl-L-aspartate3, poly-1-benzyl-L-histidine9 and poly-L-tryptophan10. It was suggested that the positive b0 value of poly-β-benzyl-L-aspartate was due to a different sense of twist3 than that found for poly-γ-benzyl-L-glutamate. Proof of this hypothesis followed shortly4,11.

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Author notes

    • GERALD D. FASMAN

    Present address: Graduate Department of Biochemistry, Brandeis University, Waltham 54, Mass.

Affiliations

  1. Children's Cancer Research Foundation, and the Harvard Medical School.

    • GERALD D. FASMAN

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https://doi.org/10.1038/193681a0

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