書誌事項

Protein folding

a discussion organized and edited by C.M. Dobson and A.R. Fersht

Cambridge University Press, c1996

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注記

First published in Philosophical transactions of the Royal Society of London, series B, volume 348 (no. 1323) pages 1-119"--CIP t.p. verso

内容説明・目次

内容説明

The ability of proteins to fold rapidly and efficiently into intricate and highly specific structures following their synthesis on ribosomes is an essential part of the conversion of genetic information into cellular activity. However, little is understood in detail of how this occurs. The Royal Society meeting on which this volume is based focused on the molecular basis of the folding processes and brought together a wide range of leading experimental and theoretical scientists in this field. This volume offers an authoritative collection of the foundations of current work. The first section discusses the experimental elucidation of the pathways of protein folding. The second section looks at theoretical approaches to folding, and the final group addresses the issue of how proteins fold in vivo. This volume will be of value to all those with an interest in protein folding, especially those in molecular biology, biochemistry and cell biology.

目次

  • Preface
  • Part I. Pathways, Kinetics and Intermediates: 1. Disulphide-coupled protein folding pathways T. Creighton
  • 2. Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution A. R. Fersht
  • 3. Insights into protein folding using physical techniques: studies of lysozyme and alpha-lactalbumin S. E. Radford and C. M. Dobson
  • 4. Initial studies of the equilibrium folding pathway of staphylococcal nuclease Yi Wang, A. T. Alexandrescu and D. Shortle
  • 5. Kinetic and equilibrium folding intermediates O. B. Ptitsym, V. E. Bychkova and V. N. Uversky
  • 6. Does the molten globule have a native-like tertiary fold? Zheng-Yu Peng, L. C. Wu, B. A. Schulman and P. S. Kim
  • Part II. Prediction, Analysis and Design: 7. Investigation of protein unfolding and stability by computer simulation W. F. van Gunsteren, P. H. Hunenberger, H. Kovacs, A. E. Mark and C. A. Schiffer
  • 8. Models of cooperativity in protein folding Hue Sun Chan, S. Bromberg and K. A. Dill
  • 9. Protein folds: towards understanding folding from inspection of native structures J. M. Thompson, D. T. Jones, M. W. MacArthur, C. M. Orengo and M. B. Swindells
  • 10. Design of two-stranded and three-stranded coiled-coil peptides S. Betz, R. Fairman, K. O'Neil, J. Lear and W. DeGrado
  • Part III. Catalysts and Chaperones: 11. Nascent chains: folding and chaperone interaction during elongation on ribosomes K. Tokatlidis, B. Friguet, D. Deville-Bonne, F. Baleux, A. N. Federov, A. Navon, L. Djavadi-Ohaniance and M. E. Goldberg
  • 12. Folding and association versus misfolding and aggregation of proteins R. Jaenicke
  • 13. Principles of chaperone-mediated protein folding F. Ulrich Hartl
  • 14. Unliganded GroEL at 2.8A: structure and functional implications P. B. Sigler and A. L. Horwich.

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詳細情報

  • NII書誌ID(NCID)
    BA28211516
  • ISBN
    • 0521576369
  • LCCN
    96015183
  • 出版国コード
    uk
  • タイトル言語コード
    eng
  • 本文言語コード
    eng
  • 出版地
    Cambridge
  • ページ数/冊数
    119 p.
  • 大きさ
    30 cm
  • 分類
  • 件名
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