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.
|Product dimensions:||5.98(w) x 9.02(h) x (d)|
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.