The structure of human apolipoprotein E2, E3 and E4 in solution. 2. Multidomain organization correlates with the stability of apoE structure
| Autor: | Alexander D. Dergunov, Michel Desmadril, Vanessa Clément-Collin, Lawrence P. Aggerbeck, Gérard Siest, Anne Barbier, Masa Takahashi, Athanase Visvikis |
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| Přispěvatelé: | Centre de génétique moléculaire (CGM), Centre National de la Recherche Scientifique (CNRS), Centre du Médicament [Nancy], Université Henri Poincaré - Nancy 1 (UHP), National Research Centre for Preventive Medicine, Moscow, National Research Centre for Preventive Medicine, Institut de biochimie et biophysique moléculaire et cellulaire (IBBMC), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), CNRS, Inserm, Caisse Nationale de l'Assurance Maladie des Travailleurs Salariés (CNAMTS), MESR, Fondation Pour la Recherche Médicale (FRM), EEC (contract MAT1-CT94046), Russian Foundation for Basic Research(grant 04-04-48165) |
| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
Protein Folding
Circular dichroism Apolipoprotein E2 Protein Conformation Apolipoprotein E4 Apolipoprotein E3 MESH: Protein Structure Secondary Biochemistry Protein Structure Secondary MESH: Circular Dichroism chemistry.chemical_compound MESH: Protein Structure Tertiary 0302 clinical medicine Protein structure MESH: Protein Conformation MESH: Spectrophotometry Ultraviolet Denaturation (biochemistry) MESH: Apolipoprotein E4 Guanidine MESH: Apolipoprotein E3 MESH: Apolipoprotein E2 0303 health sciences Circular Dichroism Temperature MESH: Chromatography Gel MESH: Apolipoproteins E Fluorescence MESH: Temperature Solutions Chromatography Gel Protein folding lipids (amino acids peptides and proteins) MESH: Spectrometry Fluorescence MESH: Protein Folding Biophysics MESH: Solutions Sensitivity and Specificity 03 medical and health sciences Apolipoproteins E Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology MESH: Particle Size Particle Size MESH: Guanidine 030304 developmental biology MESH: Humans Organic Chemistry Protein tertiary structure MESH: Sensitivity and Specificity Protein Structure Tertiary Crystallography Spectrometry Fluorescence chemistry Spectrophotometry Ultraviolet 030217 neurology & neurosurgery |
| Zdroj: | Biophysical Chemistry Biophysical Chemistry, Elsevier, 2006, 119 (2), pp.170-85. ⟨10.1016/j.bpc.2005.07.009⟩ |
| ISSN: | 0301-4622 |
| Popis: | The stabilities toward thermal and chemical denaturation of three recombinant isoforms of human apolipoprotein E (r-apoE2, r-apoE3 and r-apoE4), human plasma apoE3, the recombinant amino-terminal (NT) and the carboxyl-terminal (CT) domains of plasma apoE3 at pH 7 were studied using near and far ultraviolet circular dichroism (UV CD), fluorescence and size-exclusion chromatography. By far UV CD, thermal unfolding was irreversible for the intact apoE isoforms and consisted of a single transition. The r-apoE3 was found to be less stable as compared to the plasma protein and the stability of recombinant isoforms was r-apoE4 |
| Databáze: | OpenAIRE |
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