Amyloid, Prions, and Other Protein Aggregates

Amyloid, Prions, and Other Protein Aggregates

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This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology applications, the area in which there is the most interest, in which most of the work has already been done, and in which there is the best evidence for the structural sophisitication of the protein aggregates. The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.The plasmids pCAG20P and pCAG51P encode fusion proteins of GST and the N- terminal portion of huntingtin containing 20 ... In these proteins the proline-rich region located immediately downstream of the glutamine repeat is deleted.9 FIG. ... 20 J. Sambrook, E. F. Fritsch, and T. Maniatis, in a#39;a#39;Molecular Cloning: A Laboratory Manual, a#39;a#39; 2nd Ed. Cold Spring Harbor Laboratory Press, Plainview, NY, 1989.

Title:Amyloid, Prions, and Other Protein Aggregates
Publisher:Academic Press - 1999-09-22


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