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Conformational stability of amyloid fibrils of β2-microglobulin probed by guanidine-hydrochloride-induced unfolding
Conformational stability of amyloid fibrils of β2-microglobulin probed by guanidine-hydrochloride-induced unfolding
- Source :
- FEBS Letters. (3):313-319
- Publisher :
- Federation of European Biochemical Societies. Published by Elsevier B.V.
-
Abstract
- Although the stability of globular proteins has been studied extensively, that of amyloid fibrils is scarcely characterized. Beta2-microglobulin (beta2-m) is a major component of the amyloid fibrils observed in patients with dialysis-related amyloidosis. We studied the effects of guanidine hydrochloride on the amyloid fibrils of beta2-m, revealing a cooperative unfolding transition similar to that of the native state. The stability of amyloid fibrils increased on the addition of ammonium sulfate, consistent with a role of hydrophobic interactions. The results indicate that the analysis of unfolding transition is useful to obtain insight into the structural stability of amyloid fibrils.
- Subjects :
- Protein Denaturation
Protein Folding
Amyloid
Protein Conformation
Globular protein
Biophysics
macromolecular substances
Biochemistry
chemistry.chemical_compound
Protein structure
Structural Biology
mental disorders
Genetics
Native state
medicine
Humans
Guanidine
Molecular Biology
β2-Microglobulin
Amyloid fibrils
chemistry.chemical_classification
Beta-2 microglobulin
Amyloidosis
Cell Biology
Hydrophobic interaction
medicine.disease
Recombinant Proteins
Crystallography
Spectrometry, Fluorescence
chemistry
Ammonium Sulfate
Guanidine hydrochloride
Protein folding
beta 2-Microglobulin
Protein misfolding
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....af58761f1b2b74699b5971c28ce37ec4
- Full Text :
- https://doi.org/10.1016/j.febslet.2004.09.024