The self-association of the reduced ApoA-II apoprotein from the human high density lipoprotein complex.
The molecular properties of the single linear chain form of human apoA-II, i.e., Cm apoA-II, have been evaluated by circular dichroism, polarization of fluorescence, difference absorption, and sedimentation equilibrium. The self-association of Cm apoA-II to a dimer resembles closely that of apoA-II though the free energy change is somewhat smaller. The dimerization of Cm apoA-II is accompanied by major changes in secondary and tertiary structure. The apoA-II molecule, therefore, represents a molecular association where the intramolecular structure is strongly dependent on the quaternary structure.
D001059:Apoproteins / Q000097:blood; D002942:Circular Dichroism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008075:Lipoproteins, HDL / Q000097:blood; D046911:Macromolecular Substances; D008433:Mathematics; D008970:Molecular Weight; D011485:Protein Binding; D011487:Protein Conformation; D013696:Temperature
D001059:Apoproteins; D008075:Lipoproteins, HDL; D046911:Macromolecular Substances