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Biophys J ; 80(4): 2004-10, 2001 Apr.
Article in English | MEDLINE | ID: mdl-11259313

ABSTRACT

A mean-field theoretical approach is applied to streptavidin tetramerization and two-dimensional (2D) crystallization. This theory includes, in particular, solvent-residue interactions following the inhomogeneous Flory-Huggins model for polymers. It also takes into account residue-residue interactions by using tabulated pair interaction parameters. This theory allows one to explicitly calculate the entropy of the inhomogeneous system. We show that hydrophobic interactions are responsible for the stability of tetramerization. Within the present theory, the equilibrium distance between the two dimers is the same as that determined experimentally. The free energy of tetramerization (i.e., dissociation of the two dimers) is 50 k(B)T. Unlike tetramerization, hydrophobic interactions alone are not sufficient to stabilize the 2D crystal C(222), but solvent-mediated residue-residue interactions give the most important contribution.


Subject(s)
Streptavidin/chemistry , Crystallization , Dimerization , Indicators and Reagents/chemistry , Kinetics , Models, Chemical , Models, Molecular , Models, Statistical , Protein Binding , Protein Conformation , Protein Structure, Secondary , Protein Structure, Tertiary , Thermodynamics
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