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Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation
- Source :
- Methods in molecular biology (Clifton, N.J.). 1873
- Publication Year :
- 2018
-
Abstract
- Proteins exhibit a remarkable structural plasticity and may undergo conformational changes resulting in protein misfolding both in a biological context and upon perturbing physiopathological conditions. Such nonfunctional protein conformers, including misfolded states and aggregates, are often associated to protein folding diseases. Understanding the biology of protein folding diseases thus requires tools that allow the structural characterization of nonnative conformations of proteins and their interconversions. Here we present detailed procedures to monitor protein conformational changes and aggregation based on spectroscopic and biophysical methods that include circular dichroism, ATR-Fourier-transformed infrared spectroscopy, fluorescence spectroscopy and dynamic light scattering. To illustrate the application of these methods we report to our previous studies on misfolding, aggregation and amyloid fibril formation by superoxide dismutase 1 (SOD1), a protein whose toxic deposition is implicated in the neurodegenerative disease amyotrophic lateral sclerosis (ALS).
- Subjects :
- Models, Molecular
Protein Folding
Protein Conformation
Circular Dichroism
Amyotrophic Lateral Sclerosis
Gene Expression
Amyloidogenic Proteins
Protein Aggregation, Pathological
Anilino Naphthalenesulfonates
Dynamic Light Scattering
Recombinant Proteins
Spectrometry, Fluorescence
Superoxide Dismutase-1
Spectroscopy, Fourier Transform Infrared
Humans
Benzothiazoles
Fluorescent Dyes
Subjects
Details
- ISSN :
- 19406029
- Volume :
- 1873
- Database :
- OpenAIRE
- Journal :
- Methods in molecular biology (Clifton, N.J.)
- Accession number :
- edsair.pmid..........29aed087c678d44b1586df91f9ca8036