Protein Amyloid Aggregation : Methods and Protocols /
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| Otros Autores: | |
| Formato: | eBook |
| Lenguaje: | English |
| Publicado: |
New York, NY :
Springer New York : Imprint: Humana,
2016.
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| Edición: | 1st ed. 2016. |
| Colección: | Methods in Molecular Biology,
1345 |
| Materias: |
Tabla de Contenidos:
- Semisynthesis and Enzymatic Preparation of Post-Translationally Modified α-Synuclein
- Isotope-Labeled Amyloids Via Synthesis, Expression and Chemical Ligation for Use in FTIR, 2D IR and NMR Studies
- Inter-Molecular Paramagnetic Relaxation Enhancement (PRE) Studies of Transient Complexes in Intrinsically Disordered Proteins
- Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins
- Fluorescence Correlation Spectroscopy: A Tool to Study Protein Oligomerization and Aggregation In Vitro and In Vivo
- Deep UV Resonance Raman Spectroscopy for Characterizing Amyloid Aggregation
- Analyzing Tau Aggregation with Electron Microscopy
- Characterization of Amyloid Oligomers by Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry (ESI-IMS-MS)
- Formation and Characterization of α-Synuclein Oligomers
- Fluorescence Methods for Unraveling Oligomeric Amyloid Intermediates
- Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy
- Spin Labeling and Characterization of Tau Fibrils Using Electron Paramagnetic Resonance (EPR)
- Preparation of Crystalline Samples of Amyloid Fibrils and Oligomers
- Quenched Hydrogen Exchange NMR of Amyloid Fibrils
- Studying the Early Stages of Protein Aggregation Using Replica Exchange Molecular Dynamics Simulations
- Computational Methods for Structural and Functional Studies of Alzheimer’s Amyloid Ion Channels
- Analyzing Ensembles of Amyloid Proteins Using Bayesian Statistics
- In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar Vesicles
- Cell Models to Study Cell-to-Cell Transmission of α-Synuclein
- Preparation of Amyloid Fibrils Seeded from Brain and Meninges.