The interactions between bovine serum albumin and surfactants at pH 7 have been studied by nuclear magnetic resonance and spin‐labelling techniques. When a surfactant binds to a protein the molecular motion of all the alkyl groups of the surfactant is restricted, this effect being greater for the CH 2 near the head groups than for the CH 3 group and the intermediate CH 2 groups. The CH 2 group adjacent to the head group is in a more polar environment than the other CH 2 groups. Hence although hydrophobic bonding may account for a significant portion of the binding free energy, electrostatic forces are also important and may determine the site of the interaction.
No takes yet. Share an insight, caveat, or question.
John Oakes (1973) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: