
Sara Linse
Professor

Expression and Purification of Intrinsically Disordered Aβ Peptide and Setup of Reproducible Aggregation Kinetics Experiment
Author
Summary, in English
High purity and sequence homogeneity of intrinsically disordered proteins are prerequisites for reproducible studies of the kinetics and equilibrium of their self-assembly reactions. Starting from the pure state enables quantitative studies of intrinsic and extrinsic factors in the process to understand its molecular determinants. Here we outline detailed protocols for recombinant expression and purification of ultra-pure amyloid β peptide (Aβ) in sequence homogeneous form, which allows for the setup of reproducible kinetic self-assembly experiments.
Department/s
- Biochemistry and Structural Biology
- MultiPark: Multidisciplinary research focused on Parkinson´s disease
- NanoLund: Center for Nanoscience
Publishing year
2020
Language
English
Pages
731-754
Publication/Series
Methods in molecular biology (Clifton, N.J.)
Volume
2141
Document type
Journal article
Publisher
Springer
Topic
- Biochemistry and Molecular Biology
Keywords
- Aggregation mechanism
- Alzheimer’s disease
- Intrinsically disordered protein
- Protein expression and purification
- Reproducible kinetics experiment
- Self-assembly process
Status
Published
ISBN/ISSN/Other
- ISSN: 1940-6029