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Bibliographic Information

Mechanisms of protein folding

edited by Roger H. Pain

(Frontiers in molecular biology, 32)

Oxford University Press, 2000

2nd ed

  • : pbk

Available at  / 16 libraries

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Note

Includes bibliographical references and index

Description and Table of Contents

Volume

: pbk ISBN 9780199637881

Description

Since the publication of the first edition of mechanisms of protein folding in 1994, significant advances in both the technical and conceptual understanding of protein folding. This new edition has been brought up to date in content, context, and authorship and will make the subject accessible to a wide range of scientists. The emphasis on experimental approaches has benn maintained from the first edition but this time within the explicit context of simulations and energy surfaces. There is an introductory chapter explaining the 'new' model of protein folding, which takes into account the heterogeneity of the starting state. Advances in interpreting observed kinetic data and the development of technology to observe fast folding reactions and characterize intermediate structures have accompanied this new view and are covered in detail. The term 'molten globule'is often used incorrectly but here the significance of the term is carefully described at different satges of folding. The concept of the transition state, including the complementary approaches of molecular dynamics and protein engineering, is also discussed in detail. In vitro studies provide the molecular basis for the thermodynamic and kinetic energy minimization of the in vivo processes of protein folding and two of the potentially rate determining reactions are disulphide bond formation and proline isomerization. It has also become increasingly apparent that chaperone proteins play a vital role in protein folding and other reactions of proteins involoving major conformational change and the molecular details of these processes are discussed in detail in chapter 14. The final chapter describes the centreal importance of protein folding and unfolding reactions in disease and gives claer definition of the term 'misfolding'. Studying protein folding in vivo is full of problems and to show how these problems can be overcome in practice, three case studies of three very different types of protein have been included: the small globular protein apomyoglobin; the fibrous protein collagen; and the membrane protein haemagglutinin.
Volume

ISBN 9780199637898

Description

Protein folding is the process by which newly synthesized polypeptide chains become their final 3 dimensional protein forms. Mechanisms of Protein Folding 2e makes this complex subject accessible to scientists from various backgrounds.

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Details

  • NCID
    BA51124503
  • ISBN
    • 019963789X
    • 0199637881
  • LCCN
    00058882
  • Country Code
    uk
  • Title Language Code
    eng
  • Text Language Code
    eng
  • Place of Publication
    Oxford ; New York
  • Pages/Volumes
    xxvi, 433 p.; 26 cm
  • Classification
  • Subject Headings
  • Parent Bibliography ID
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