The role that primary amino acid sequences plays in influencing the partitioning of polypeptides between productive folding and irreversible aggregation pathways has introduced a whole new dimension to the folding problem. The volume deals with the structures of the products of protein misassembly and the role of amino acid sequences in favoring these structures.


Molecular biologists, biochemists, immunologists, and biophysicists.

Table of Contents

R. Jaenicke and R. Seckler, Protein Misassembly in Vitro. M.P. Schlunegger, M.J. Bennett, and D. Eisenberg, Oligomer Formation by 3D Domain Swapping: A Model for Protein Assembly and Misassembly. M. Sunde and C. Blake, The Structure of Amyloid Fibrils by Electron Microscopy and X-Ray Diffraction. W. Colon, Z. Lai, H.A. Lashuel, J. McCulloch, S.L. McCutchen, G.J. Miroy, S.A. Peterson, and J.W. Kelly, Transthyretin Quaternary and Tertiary Structural Changes Facilitate Misassembly into Amyloid. R. Wetzel, Domain Stability in Immunoglobulin Light Chain Deposition Disorders. S. Betts, C. Haase-pettingel, and J. King, Mutational Effects on Inclusion Body Formation. Author Index. Subject Index.


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© 1997
Academic Press
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About the serial-volume-editor


@qu:"The authority, originality, and editing of the reviews are first class." @source:--NATURE @qu:"The Advances in Protein Chemistry series has been a major factor in the education of protein chemists." @source:--JOURNAL OF THE AMERICAN CHEMICAL SOCIETY @qu:"...this book provides a revealing and up-to-date look at many aspects of protein aggregation and amyloid fibril formation...will be invaluable for anyone, and especially newcomers interested in the structure of amyloid and its molecular basis." @source:—Anthony L. Fink, Ph.D., University of California, Santa Cruz, in AMYLOID (1999)