Protein Stability and Folding

1. Front Matter

   Pages i-x

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2. Noncovalent Forces Important to the Conformational Stability of Protein Structures

   • Kenneth P. Murphy

   Pages 1-34

3. Degradative Covalent Reactions Important to Protein Stability

   • David B. Volkin, Henryk Mach, C. Russell Middaugh

   Pages 35-63

4. Fluorescence Spectroscopy

   • Catherine A. Royer

   Pages 65-89

5. Ultraviolet Absorption Spectroscopy

   • Henryk Mach, David B. Volkin, Carl J. Burke, C. Russell Middaugh

   Pages 91-114

6. Circular Dichroism

   • Kunihiro Kuwajima

   Pages 115-135

7. Infrared Spectroscopy

   • C. Russell Middaugh, Henryk Mach, James A. Ryan, Gautam Sanyal, David B. Volkin

   Pages 137-156

8. Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide Mapping

   • Kenneth R. Williams, Kathryn L. Stone

   Pages 157-175

9. Urea and Guanidine Hydrochloride Denaturation Curves

   • Bret A Shirley

   Pages 177-190

10. Differential Scanning Calorimetry

    • Ernesto Freire

    Pages 191-218

11. Disulfide Bonds in Protein Folding and Stability

    • Nigel Darby, Thomas E. Creighton

    Pages 219-252

12. Solvent Stabilization of Protein Structure

    • Serge N. Timasheff

    Pages 253-269

13. Site-Directed Mutagenesis to Study Protein Folding and Stability

    • Philip N. Bryan

    Pages 271-289

14. Hydrogen Exchange Techniques

    • J. Martin Scholtz, Andrew D. Robertson

    Pages 291-311

15. Protein Folding Kinetics

    • Thomas Kiefhaber

    Pages 313-341

16. Molten Globules

    • Anthony L. Fink

    Pages 343-360

17. Chaperonin-Assisted Protein Folding of the Enzyme Rhodanese by GroEL/GroES

    • Paul M. Horowitz

    Pages 361-368

18. Back Matter

    Pages 369-377

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The intent of this work is to bring together in a single volume the techniques that are most widely used in the study of protein stability and protein folding. Over the last decade our understanding of how p- teins fold and what makes the folded conformation stable has advanced rapidly. The development of recombinant DNA techniques has made possible the production of large quantities of virtually any protein, as well as the production of proteins with altered amino acid sequence. Improvements in instrumentation, and the development and refinement of new techniques for studying these recombinant proteins, has been central to the progress made in this field. To give the reader adequate background information about the s- ject, the first two chapters of this book review two different, yet related, aspects of protein stability. The first chapter presents a review of our current understanding of the forces involved in determining the conf- mational stability of proteins as well as their three-dimensional folds. The second chapter deals with the chemical stability of proteins and the pathways by which their covalent structure can degrade. The remainder of the book is devoted to techniques used in the study of these two major areas of protein stability, as well as several areas of active research. Although some techniques, such as X-ray crystallography and mass spectroscopy, are used in the study of protein stability, they are beyond the scope of this book and will not be covered extensively.

...very useful for any biochemist who needs to understand concepts of protein folding and stability and how protein folding can be monitored and studied. This is a good book for student researchers and should be considered as an addition to courses on protein structure.-Doody's Health Sciences Book Review Journal

• Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield

  Bret A. Shirley

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