
pmid: 5016554
AbstractConformational change of histone IV, induced by phosphate, have been investigated by observing the intrinsic fluorescence of tyrosine residues and circular dichroism (CD). There is a fast conformational change upon the addition of phosphate, followed by a slow process with time constants in the range of minutes to hours depending upon both the phosphate and histone concentrations. The CD results indicate α‐helix formation in the fast process, and β‐sheet formation in the slow one, although other secondary and tertiary structural changes also may occur. The histone concentration dependence of the fast process is consistent with dimerization. Divalent phosphate is about ten times more effective than monovalent phosphate in inducing conformational changes. All of the changes are reversible.
Histones, Protein Conformation, Circular Dichroism, Osmolar Concentration, Electrochemistry, Tyrosine, Fluorescence, Phosphates
Histones, Protein Conformation, Circular Dichroism, Osmolar Concentration, Electrochemistry, Tyrosine, Fluorescence, Phosphates
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