Mechanisms of protein folding
By: edited by Roger H. Pain.
Contributors: Pain, Roger H.
Edition: 2nd ed.
Series: Frontiers in molecular biology -- 32.
Publisher: Oxford University Press
Published: 2000
Place of publication: Oxford; New York
Language: eng
Number of pages: 433
Subjects: Protein folding.
Notes: Includes bibliographical references and index.
Table of contents: title: The nature and significance of protein folding / Christopher M. Dobson; title: Kinetic models in protein folding / Oliver Bieri and Thomas Kiefhaber; title: Early stages of protein folding / Heinrich Roder, Gülnur A. Elöve, and M.C. Ramachandra Shastry; title: Protein folding monitored by mass spectrometry / Carol V. Robinson; title: Folding events in the submillisecond range / Martin Gruebele; title: The molten globule state : the physical picture and biological significance / Kunihiro Kuwajima and Muneihito Arai; title: Transition states in protein folding / Valerie Daggett and Alan R. Fersht; title: Proline isomerization and its catalysis in protein folding / Jochen Balbach and Franz X. Schmid; title: Protein folding coupled to disulphide-bond formation / Thomas E. Creighton; title: Assembly of multi-subunit structures / Robert Seckler; title: Case study 1 : The folding process of apomyoglobin / Peter E. Wright and Robert L. Baldwin; title: Case study 2 : Folding of the collagen triple-helix and its naturally occurring mutants / Jean Baum and Barbara Brodsky; title: Case study 3 : Folding of influenza haemagglutinin in the living cell / Lars Ellgaard and Ari Helenius; title: Cellular functions of molecular chaperones / Michel R. Leroux and F. Ulrich Hartl; title: Protein folding and human disease / Stephen W. Raso and Jonathan King.