Conformational changes of proteins at an interface induced by a supported planar phosphatidic acid monolayer.
Conformational changes of two types of proteins, water-soluble proteins (BSA and myoglobin) and membrane-associated protein (cytochrome c), induced by a negatively charged supported planar phospholipid monolayer were studied. The water-soluble proteins lost most of their ordered secondary structure and formed a random conformation in the initial stage of adsorption, and but in the later stage they retained more of the alpha-helical structure which was their main native secondary structure in solution. The membrane-associated protein, cytochrome c, showed a different conformational change in the adsorption process. In the initial stage, it showed an increase in beta-structures but not random coils. In the later stage, it contained more alpha-helixes than that in solution.
Sui
S F
SF
Department of Biological Sciences & Biotechnology, Tsinghua University, Beijing, People's Republic of China.
Wu
H
H
Sheng
J
J
Guo
Y
Y
D000327:Adsorption; D002942:Circular Dichroism; D003574:Cytochrome c Group / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D010712:Phosphatidic Acids / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D012995:Solubility
D003574:Cytochrome c Group; D009211:Myoglobin; D010712:Phosphatidic Acids; D012710:Serum Albumin, Bovine