Influence of the protein conformation on the interaction between α-lactalbumin and dimyristoylphosphatidylcholine vesicles

Membrane-protein interaction and the molten globule state: Interaction of α-lactalbumin with membranes

“…6). The CD at low pH is similar in the far-UV region to that reported earlier (Robbins and Holmes, 1970;Hanssens et at., 1985), but very different in the near-UV region. The absence of near-UV CD in the low-pH region is in keeping with the absence of any stable tertiary structure in the molten globule state.…”

Interaction of bovine -lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy

“…However, at acid pH (o4), hydrophobic forces dominate the interaction and the vesicles are solubilized. This fact suggests that at low pH, alactalbumin behaves as an intrinsic membrane protein (Hanssens, van Ceunebroek, Pottel, Preaaux, & van Cauwelaert, 1985;Cawthern, Permyakov, & Berliner, 1996).…”

Conformational States and Thermodynamics of α-Lactalbumin Bound to Membranes: A Case Study of the Effects of pH, Calcium, Lipid Membrane Curvature and Charge

“…The interactions of BLA with large unilamellar vesicles (LUVs) as well as with small unilamellar vesicles (SUVs) has been the subject of numerous studies. 21,[32][33][34][35][36][37][38][39] The amphiphilic a-helices aA and aC have been identified as the anchoring sites of BLA to SUVs by photochemical labelling and more recently by H/ 2 H-exchange experiments. 32,35 However, the state of the membranebound protein is still unclear.…”