A theoretical approach to the binding of amphipathic molecules to globular proteins.
1. A theory based on a multiple equilibrium model with stoicheiometric binding constants has been formulated. It is applicable to the interaction of amphipathic molecules with charged macromolecules. 2. The theory has been applied to the binding of sodium n-dodecyl sulphate to ribonuclease A, beta-lactoglobulin and bovine serum albumin. 3. Over the ranges of surfactant concentration where binding is non-co-operative and co-operative, the experimental data can be satisfactorily fitted with energy and co-operatively parameters which are of comparable magnitude for the three globular proteins. 4. The results imply that the energy of interaction of sodium n-dodecyl sulphate with the proteins is equivalent to the formation of approximately four CH2 hydrophobic bonds.
D007782:Lactoglobulins / Q000378:metabolism; D046911:Macromolecular Substances; D008956:Models, Chemical; D011485:Protein Binding; D012260:Ribonucleases / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000378:metabolism; D012967:Sodium Dodecyl Sulfate / Q000378:metabolism
D007782:Lactoglobulins; D046911:Macromolecular Substances; D012710:Serum Albumin, Bovine; D012967:Sodium Dodecyl Sulfate; D012260:Ribonucleases