Mechanisms of protein folding / edited by Roger H. Pain.

2nd ed.
Oxford ; New York : Oxford University Press, 2000.
xxvi, 433 pages, [16] pages of color plates : illustrations ; 25 cm.


Summary note
  • "The process by which newly synthesized polypeptide chains become their final 3-dimensional protein forms is clearly explained, providing students and researchers of various backgrounds with both a conceptual and technical understanding of the subject. The new Second Edition incorporates the significant improvements in the field such as advances in interpreting observed kinetic data, the development of technology to observe fast folding reactions, the molten globule state, and the vital role of chaperone proteins in protein folding. The emphasis on experimental approaches has been maintained but this edition does so within the explicit context of simulations and energy surfaces.
  • New discoveries of the central importance of protein folding and unfolding reactions in biology and medicine (including mutation and 'misfolding') are carefully explored. Three case studies elucidate the difficulties of studying protein folding in vivo."--Jacket.
Bibliographic references
Includes bibliographical references and index.
  • The nature and significance of protein folding / Christopher M. Dobson
  • Kinetic models in protein folding / Oliver Bieri and Thomas Kiefhaber
  • Early stages of protein folding / Heinrich Roder, Gülnur A. Elöve, and M.C. Ramachandra Shastry
  • Protein folding monitored by mass spectrometry / Carol V. Robinson
  • Folding events in the submillisecond range / Martin Gruebele
  • The molten globule state : the physical picture and biological significance / Kunihiro Kuwajima and Muneihito Arai
  • Transition states in protein folding / Valerie Daggett and Alan R. Fersht
  • Proline isomerization and its catalysis in protein folding / Jochen Balbach and Franz X. Schmid
  • Protein folding coupled to disulphide-bond formation / Thomas E. Creighton
  • Assembly of multi-subunit structures / Robert Seckler
  • Case study 1 : The folding process of apomyoglobin / Peter E. Wright and Robert L. Baldwin
  • Case study 2 : Folding of the collagen triple-helix and its naturally occurring mutants / Jean Baum and Barbara Brodsky
  • Case study 3 : Folding of influenza haemagglutinin in the living cell / Lars Ellgaard and Ari Helenius
  • Cellular functions of molecular chaperones / Michel R. Leroux and F. Ulrich Hartl
  • Protein folding and human disease / Stephen W. Raso and Jonathan King.
  • 0199637881 ((pbk. ; : alk. paper))
  • 9780199637881 ((pbk. ; : alk. paper))
  • 019963789X ((hbk.))
  • 9780199637898 ((hbk.))
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