Magnetic circular dichroism of netropsin and natural circular dichroism of the netropsin-DNA complex

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Abstract
The 1st measurement of the magnetic circular dichroism (MCD) of the basic polypeptide antibiotic netropsin (Nt) is reported. The MCD shows that the longest wavelength absorption band of Nt is the sum of > 1 component and permits a radically new interpretation of the circular dichroism of the complex which Nt forms with DNA. Nt apparently has no major effect on the CD and the helical structure of the bases of the DNA to which it is bound. The ability of Nt to inhibit the function of DNA polymerase, RNA polymerase and the photoreactivating enzyme may be mediated by factors other than a distortion of the helical structure of the bases.

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