Protein Amyloid Aggregation

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.