Unfolding of a leucine zipper is not a simple two-state transition.

Abstract

Temperature-induced unfolding of the leucine zipper, an alpha-helical, double-stranded, coiled-coil, was studied by circular dichroism spectroscopy, spectrofluorimetry and heat capacity scanning calorimetry. It is shown that this process does not represent a simple two-state transition, as previously believed, but consists of several stages. The first… (More)

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