Protein folding
Author(s)
Bibliographic Information
Protein folding
W.H. Freeman, c1992
Available at 35 libraries
  Aomori
  Iwate
  Miyagi
  Akita
  Yamagata
  Fukushima
  Ibaraki
  Tochigi
  Gunma
  Saitama
  Chiba
  Tokyo
  Kanagawa
  Niigata
  Toyama
  Ishikawa
  Fukui
  Yamanashi
  Nagano
  Gifu
  Shizuoka
  Aichi
  Mie
  Shiga
  Kyoto
  Osaka
  Hyogo
  Nara
  Wakayama
  Tottori
  Shimane
  Okayama
  Hiroshima
  Yamaguchi
  Tokushima
  Kagawa
  Ehime
  Kochi
  Fukuoka
  Saga
  Nagasaki
  Kumamoto
  Oita
  Miyazaki
  Kagoshima
  Okinawa
  Korea
  China
  Thailand
  United Kingdom
  Germany
  Switzerland
  France
  Belgium
  Netherlands
  Sweden
  Norway
  United States of America
Note
Includes bibliographical references and index
Description and Table of Contents
Description
The phenomenon of protein folding has become the focus of intense scientific inquiry. Researchers have realised the importance of understanding how proteins adopt their folding conformations, and are developing experimental techniques to attack this problem. , Protein Folding is a report on the current state of this crucial area of research-the 4y experiments, techniques, and implications of recent findings on modem biotechnology and biomedicine. Its authors are the world's leading investigators in this field, including: R M. Richards, Department of Molecular Biophysics and Biochemistry, Yale University - Janet M Thornton, Biomolecular Structure and Modelling Unit, University College,. . London, UK - Peter L Privokv, Institute of Protein Research, Academy of Sciences, Moscow - Martin Karplus and E. S h, Department of Chemistry, Harvard University - Franz X Schmid, Department of Biochemistry, Universitat Bayreuth, Germany . Oleg B. Ptilsyn, Institute of Protein Research, Academy of Sciences, Moscow Thomas E. Creighton, European Molecular Biology Laboratory, Heidelberg, Germany David P.
Goldenberg, Department of Biology, University of Utah - Jean-Renaud Garel, Laboratoire d'Enzymologie du CNRS, Gifsur-Yvette, France - Robert B. Freedman, Biological Laboratory, University of Kent, Canterbury, UK.
Table of Contents
- I Folded and Unfolded Proteins-An Introduction
- The Folding Reaction
- Restrictions on Local Conformations
- The Unfolded (Denatured) State
- The Folded (Native) State
- Intermediate States
- The Solvent
- 2 Protein Structures-The End Point of the Folding Pathway
- Dihedral Angles
- Glycine Residues
- Proline Residues
- Side Chain Interactions
- Secondary Structure
- Loop Regions
- Salvation
- Topology
- Comparison of Similar Structures
- 3 Physical Basis of the Stability of the Folded Conformations of Proteins
- General Specification of a Protein Molecule as a Physical Object
- Intramolecular Forces in Proteins
- Theoretical and Practical Problems in Studying Protein Folding
- Cooperativity of Denaturation
- Denatured States of Proteins
- Enthalpy and Entropy Differences of the Native and Denatured State of Proteins
- Stability of the Native State
- Cold Denaturation of Proteins
- Denaturation Heat Capacity Increment
- Hydration of Nonpolar Groups
- Hydration of Protein Groups
- Mechanism of Stabilization of the Native Protein Structure
- Conclusion
- 4 Protein Folding: Theoretical Studies of Thermodynamics and Dynamics
- Methods
- Protein Thermodynamics
- Dynamic Aspects of Protein Folding
- Conclusion
- 5 Kinetics of Unfolding and Refolding oi Single-Domain Proteins
- The Cooperativity of Folding and Its Kinetic Implications
- Folding and Prollyl Peptide Bond Isomerization
- Kinetic Properties of Folding Reactions
- Folding Intermediates
- Transition State for Folding
- Case Studies
- Folding Mechanism of Small Proteins: Perspectives
- 6 The Molten Globule State
- Background
- Properties of the Molten Globule
- Model of the Molten Globule
- Transitions Between Conformational States
- Occurrence of the Molten Globule
- Protein Folding
- Possible Roles oi the Molten Globule
- Conclusions
- 7 Folding Pathways Elucidated Using Disulfide Bonds
- Disulfide Bond Formation as a Probe of Protein Conformational Transitions
- Folding Pathways Elucidated Using Disulfide Bonds
- General Lessons from Disulficle Folding Pathways
- Summary
- 8 Mutational Analysis of Protein Folding and Stability
- Strategies and Methodologies for Mutational Anaiysis of Folding
- Mutational Analysis of the Contributions of Individual Interactions to Protein Stability
- MutationaiAnalysis of Folding Transition States and Intermediates
- Effects of Mutations on the Conformations of Folded and Unfolded Proteins
- Effects of Mutations on Protein Folding and Assembly in vivo
- 9 Large Multidomain and Multisubunit Proteins
- Multidomain Single-Chain Proteins
- Oligometric Proteins
- Extrapolation to Folding in vivo of the Results Obtained in vitro
- with Large Proteins General Conclusions and Perspectives
- 10 Protein Folding in the Cell
- Protein Folding in the Context of Protein Biosynthesis
- Protein Misfolding: Insight into Protein Folding in the Cell
- Cellular Catalysis of Protein Folding
- Protein Fouling and Protein Traffic in the Cell: General Considerations
- part cont.
by "Nielsen BookData"