Protein misassembly

Author(s)

• Wetzel, Ronald

Bibliographic Information

Protein misassembly

edited by Ronald Wetzel

（Advances in protein chemistry / edited by M.L. Anson, John T. Edsall, Kenneth Bailey, v. 50）

Academic Press, c1997

Note

Includes bibliographical references and author and subject indexes

Description and Table of Contents

Description

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.

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.

by "Nielsen BookData"

Details

• NCID: BA3277106X
• ISBN:
  • 0120342502
• Country Code: us
• Title Language Code: eng
• Text Language Code: eng
• Place of Publication: San Diego
• Pages/Volumes: xx, 282 p., [12] p. of color plates
• Size: 24 cm
• Classification:
  • DC21 : 572.633
• Subject Headings:
  • LCSH : Protein folding
  • LCSH : Proteins -- Structure
• Parent Bibliography ID:
  • BA00323750