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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 C (volume 413) 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 c

Amyloid beta-protein. --- Amyloid. --- Cell Aggregation. --- Prions. --- Proteins. --- Amyloid --- 547.458.83 --- metabolism. --- Amyloids --- 547.458.83 Amyloids --- Infectious protein particles --- Prion proteins --- Protein particles, Infectious --- Proteinaceous infection particles --- PrP proteins --- Alzheimer beta-protein --- Amyloid fibril protein (Alzheimer's) --- Amyloid protein A4 --- Beta-amyloid protein --- Amyloid beta-protein precursor --- Amyloïde beta-proteïnenprecursor --- Precursor [Amyloïde beta-proteïnen] --- Prions --- Protein engineering --- Protein particles [Infectious ] --- Proteïnen--Engineering --- Protéines--Ingénierie --- Précurseur amyloïde bêta-protéinique --- Amyloid beta-protein Amyloid Prions. --- -#WSCH:FYS3 --- Proteins --- Congresses --- Glycoproteins --- Enzymes. --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- metabolism --- -metabolism --- Aggregates --- Aggregation --- Protein structure