Monitoring the Interaction between β(2)-Microglobulin and the Molecular Chaperone αB-crystallin by NMR and Mass Spectrometry: αB-CRYSTALLIN DISSOCIATES β(2)-MICROGLOBULIN OLIGOMERS

The interaction at neutral pH between wild-type and a variant form (R3A) of the amyloid fibril-forming protein β(2)-microglobulin (β2m) and the molecular chaperone αB-crystallin was investigated by thioflavin T fluorescence, NMR spectroscopy, and mass spectrometry. Fibril formation of R3Aβ2m was pot...

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Détails bibliographiques
Auteurs principaux: Esposito, Gennaro, Garvey, Megan, Alverdi, Vera, Pettirossi, Fabio, Corazza, Alessandra, Fogolari, Federico, Polano, Maurizio, Mangione, P. Patrizia, Giorgetti, Sofia, Stoppini, Monica, Rekas, Agata, Bellotti, Vittorio, Heck, Albert J. R., Carver, John A.
Format: Artigo
Langue:Inglês
Publié: American Society for Biochemistry and Molecular Biology 2013
Sujets:
Molecular Biophysics
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC3682583/
https://ncbi.nlm.nih.gov/pubmed/23645685
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M112.448639
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