Abstract
The cooperative binding of histone H1 to polynucleosome was studied quantitatively. The equilibrium and kinetic data were satisfactorily described in terms of the large ligand model. The binding constant K and the cooperativity parameter q showed remarkable salt effects: K = 7.5 × 107 M−1 and q = 1.3 × 104 at 0.2 M NaCl, pH 7.5 and 20°C. This considerably strong cooperativity reveals that the polynucleosome state, condensed or not, is sensitive to small changes in he free histone H1 concentration around the value of 1/K. The association rate constant was of the order of 107 M−1·s−1 and had a small salt concentration dependence, indicating a diffusion‐controlled association process.