Protein Amyloid Aggregation

Methods and Protocols

Buch | Softcover

314 Seiten

2016 | Softcover reprint of the original 1st ed. 2016
Humana Press Inc. (Verlag)
978-1-4939-5005-8 (ISBN)

Artikel merken

This detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers which feature in the etiology of a variety of human disorders collectively known as amyloidoses. The scope of the collection includes techniques for visualizing early steps on the amyloid formation pathway, methods for capturing and characterizing oligomeric, potentially toxic, intermediates, strategies for preparing and characterizing mature amyloid fibrils and approaches for understanding templating and transmission of amyloid aggregates. Written in the highly successful Methods in Molecular Biology series format, the chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols and tips on troubleshooting and avoiding known pitfalls.

Authoritative and practical, Protein Amyloid Aggregation: Methods and Protocols serves as an ideal guide for biochemists and biophysicists with an interest in elucidating the mechanisms of protein amyloid formation, as well as chemists, pharmacologists and clinicians with an interest in leveraging an understanding of such mechanisms for the purpose of therapeutic development.

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.

Erscheinungsdatum	19.08.2017
Reihe/Serie	Methods in Molecular Biology ; 1345
Zusatzinfo	49 Illustrations, color; 24 Illustrations, black and white; XIV, 314 p. 73 illus., 49 illus. in color.
Verlagsort	Totowa, NJ
Sprache	englisch
Maße	178 x 254 mm
Themenwelt	Naturwissenschaften ► Biologie ► Allgemeines / Lexika
	Naturwissenschaften ► Biologie ► Biochemie
	Naturwissenschaften ► Biologie ► Mikrobiologie / Immunologie
Schlagworte	Aggregation processes • amyloid fibrils • Amyloid formation pathway • Amyloidoses • human disease • pharmacology • Therapeutic development • Toxicity
ISBN-10	1-4939-5005-3 / 1493950053
ISBN-13	978-1-4939-5005-8 / 9781493950058
Zustand	Neuware