Native like structure and stability of apo AI in an-propanol/water solution as determined by13C NMR
- 7 March 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 361 (1) , 29-34
- https://doi.org/10.1016/0014-5793(95)00134-u
Abstract
To elucidate the molecular details of the conformation of apolipoprotein AI (apo AI), we have developed an approach related to the solubilization of this protein in 30% n-propanol. We have previously reported the promotion of a native-like structure for apo AI solubilized in n-propanol, as depicted by circular dichroism, fluorescence, and limited proteolytic digestion as compared to the lipid associated form of apo AI. In the present study, we labeled the Lys residues of apo AI with 13C by reductive methylation and used 13C NMR to confirm the formation of a native-like structure of apo AI in this environment. Furthermore, by the above criteria (circular dichroism and 13C NMR) and by using urea and temperature as denaturing agents, we show that the denaturation of the native-like structure of apo AI in n-propanol is a biphasic process. These studies show that in 30% n-propanol, apo AI contains two independently folded structural domains, of markedly different stabilities that might correspond to the amino-terminal and the carboxy-terminal halves of the moleculeKeywords
This publication has 11 references indexed in Scilit:
- Native-like structure and self-association behavior of apolipoprotein A-I in a water/n-propanol solutionBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1994
- Crystallization and Preliminary X-ray Analysis of Human Plasma Apolipoprotein C-IJournal of Molecular Biology, 1994
- Three-Dimensional Structure of the LDL Receptor-Binding Domain of Human Apolipoprotein EScience, 1991
- Crystallization and preliminary X-ray diffraction studies on the amino-terminal (receptor-binding) domain of human apolipoprotein E3 from serum very low density lipoproteinsJournal of Molecular Biology, 1988
- Anion-exchange fast protein liquid chromatographic characterization and purification of apolipoproteins A-I, A-II, C-I, C-II, C-III0, C-III1, C-III2 and E from human plasmaJournal of Chromatography B: Biomedical Sciences and Applications, 1987
- [29] Spectroscopic studies of lipoproteinsPublished by Elsevier ,1986
- Effects of amino group modification in discoidal apolipoprotein A-I-egg phosphatidylcholine-cholesterol complexes on their reactions with lecithin:cholesterol acyltransferaseBiochemistry, 1985
- Methyl motions in 13C-methylated concanavalin as studied by carbon-13 magnetic resonance relaxation techniquesBiochemistry, 1984
- Mechanism of dissociation of human apolipoproteins A-I, A-II, and C from complexes with dimyristoylphosphatidylcholine as studied by thermal denaturationBiochemistry, 1984
- Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersionBiochemistry, 1972