Solvent binding sites

Zhang, X.J., and Matthews, B. W. (1994). Conservation of solvent-binding sites in 10 crystal forms of t4 lysozyme. Protein Sd. 3,1031-1039. 

In conclusion, the generation of solvento-complexes as reactive intermediates is extensively used in synthesis. Three distinct approaches have been developed to provide solvent-binding sites (i) conversion of ligands into products with low solubility or their transformation into volatile compounds, (ii) chemical transformations of coordinated ligands where the products of the reaction are poorer donors and are expelled from the coordination sphere of the complex, and (Hi) manipulation of the metal oxidation state to affect ligand-binding properties. 

Often the materials swell to different extents depending on the type of diluent. The swelling is here normally high in solvents and low in nonsolvents for the polymer. Unfortunately, this may lead to large changes in the accessibility and density of the binding sites when the solvent is changed [16]. 

The very high resolution for the ESR spectrum of cob(II)alamin in the enzyme system is undoubtedly due to the fact that all the coenzyme molecules are bound in an identical environment at the enzyme active site. This results in a homogeneous cobalt-benzimidazole geometry, because both identical binding sites, solvent, and solute molecules can no longer approach the Bia-molecule closely. In addition, the enzyme bound cob(II)alamin molecules are more isolated from one another and thus relaxation due to spin-spin interactions is less effective in broadening spectral lines. 

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