AMYLOID, PRIONS, AND OTHER PROTEIN AGGREGATES, PART C, 413
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Ronald Wetzel, University of Tennessee Medical Center, Knoxville, U.S.A. Indu Kheterpal
Description The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly
recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part B (volume 412) on Amyloid,
Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological
insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological
activities of this important class of protein assemblies.
Audience
Biochemists, cell biologists, neuroscientists, and related fields engaged in protein research.
Contents
Characterization of protein deposition in vitro.
Chapter 1: Purification of Polyglutamine Proteins
Chapter
2: Preparation of amyloid beta-protein for structural and functional studies.
Chapter 3: Kinetics and thermodynamics of amyloid assembly
using an HPLC-based sedimentation assay. Chapter 4: Protein aggregation starting from the native, globular stete.
Chapter 5: Direct
observation of amyloid growth monitored by total internal reflection fluorescence microscopy.
Chapter 6: Characterization of Amyloid
Structures at the Molecular Level by Solid State Nuclear Magnetic Resonance Spectroscopy.
Chapter 7: Spin Labeling Analysis of Amyloids
and other Protein Aggregates.
Chapter 8: Hydrogen-Deuterium Exchange Mass Spectrometry of Protein Aggregates.
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