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...

Full description

Saved in:
Bibliographic Details
Main Authors: 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
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2013
Subjects:
Molecular Biophysics
Online Access: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
Tags: Add Tag
No Tags, Be the first to tag this record!

Similar Items