Title | Protein Amyloid Aggregation [electronic resource] : Methods and Protocols / edited by David Eliezer |
---|---|
Imprint | New York, NY : Springer New York : Imprint: Humana Press, 2016 |
Edition | 1st ed. 2016 |
Connect to | http://dx.doi.org/10.1007/978-1-4939-2978-8 |
Descript | XIV, 314 p. 73 illus., 49 illus. in color. online resource |
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