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Interaction of native and partially folded conformations of α‐lactalbumin with lipid bilayers: characterization of two membrane‐bound states
Author(s) -
Bañuelos Sonia,
Muga Arturo
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00406-1
Subject(s) - bilayer , conformational isomerism , lipid bilayer , chemistry , membrane , adsorption , crystallography , lactalbumin , biophysics , molecule , organic chemistry , chromatography , biochemistry , biology
α‐Lactalbumin (αLA) can adopt two different membrane‐bound states depending on the physical properties of the lipid bilayer, namely adsorbed and inserted. The latter, but not the adsorbed state, is able to disrupt the permeability barrier of the bilayer. The structure of both states is strongly affected by the conformational properties of the αLA conformer considered: as protein flexibility increases the helical content of the membrane‐bound conformation decreases, especially in the adsorbed form. Moreover, the adsorbed and the inserted states of those conformers containing 3 or 4 disulfides can interconvert in response to changes in the physical properties of the host membrane.