Link to Pubmed [PMID] – 15893324
J. Mol. Biol. 2005 Jun;349(4):890-905
The study of the conformational changes of bovine alpha-lactalbumin, switching from soluble states to membrane-bound states, deepens our knowledge of the behaviour of amphitropic proteins. The binding and the membrane-bound conformations of alpha-lactalbumin are highly sensitive to environmental factors, like calcium and proton concentrations, curvature and charge of the lipid membrane. The interactions between the protein and the membrane result from a combination of hydrophobic and electrostatic interactions and the respective weights of these interactions depend on the physicochemical conditions. As inferred by macroscopic as well as residue-level methods, the conformations of the membrane-bound protein range from native-like to molten globule-like states. However, the regions anchoring the protein to the membrane are similar and restricted to amphiphilic alpha-helices. H/(2)H-exchange experiments also yield residue-level data that constitute comprehensive information providing a new point of view on the thermodynamics of the interactions between the protein and the membrane.