Abstract
Two types of nucleoproteins, viz. reconstituted SV 40 minichromosomes and polymers of chromatin subunits (polynucleosomes), were studied by sedimentation velocity analysis in relation to the ionic strength. The representation of the sedimentation coefficients s20,wapp as a function of the Debye-Hückel electrostatic sreening radius 1/κ has revealed interesting structural properties: in both systems several quasi-linear curve segments have been obtained which might represent different structural states. These states reflect extended, condensed and associated nucleoprotein conformations. The transitions between these states are characterized by sharp kink-points representing drastic conformational changes, possibly with a cooperative character. They are discussed in terms of the polyelectrolyte theory. The presence of histone H1 modifies these plots in regard to a stabilization of the condensed forms.
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