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- W2896878547 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)." @default.
- W2896878547 created "2018-10-26" @default.
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- W2896878547 date "2018-10-20" @default.
- W2896878547 modified "2023-09-23" @default.
- W2896878547 title "Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation" @default.
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- W2896878547 doi "https://doi.org/10.1007/978-1-4939-8820-4_1" @default.
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