Abstract
RECENTLY in solutions of α-helical polypeptides and proteins a Cotton effect was observed, having an inflexion point at 225 mµ and which has been shown to be conformation-dependent1–3. This Cotton effect probably plays a major part in determining the shape of the rotatory dispersion curve in the visible region and therefore is responsible for the Moffitt term, which has been the empirical factor in estimates of the helical contents of polypeptides4. We wish to report here a sensitive method for studying the conformation of polypeptides by using the circular dichroism (C.D.) measurements10 in the ultra-violet region of this Cotton effect at 225 mµ. The surface of the C.D. bands (a measure of the rotational strength) can be correlated with the amount of helical content, while the sign of C.D. bands might be related to the absolute conformation, that is, the sense of helix.
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References
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BRAHMS, J., SPACH, G. Circular Dichroic Studies of Synthetic Polypeptides. Nature 200, 72–73 (1963). https://doi.org/10.1038/200072a0
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DOI: https://doi.org/10.1038/200072a0
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