Library Science

In Protein Stability and Folding: Theory and Practice, world-class scientists present in a single volume a comprehensive selection of hands-on recipes for all of the major techniques needed to understand the conformational stability of proteins, as well as their three-dimensional folding. The distinguished contributors provide clear, step-by-step instructions along with many troubleshooting tips, alternative procedures, and informative explanations about why certain steps are necessary. Even highly skilled researchers will find many time-saving methods. Among the techniques discussed are fluorescent, ultraviolet, and infrared spectroscopy; HPLC peptide mapping; differential scanning calorimetry; and hydrogen exchange. Shirley’s Protein Stability and Folding: Theory and Practice will ensure a significant difference in the outcome of your experiments, producing the result desired even for beginners.

Authors: Shirley, Bret A.

Download Book (PDF 22233K)

Table of Contents

1. Noncovalent Forces Important to the Conformational Stability of Protein Structures (pp. 1-34)
   Murphy, Kenneth P.
2. Degradative Covalent Reactions Important to Protein Stability (pp. 35-64)
   Volkin, David B.; Mach, Henryk; Middaugh, C. Russell
3. Fluorescence Spectroscopy (pp. 65-90)
   Royer, Catherine A.
4. Ultraviolet Absorption Spectroscopy (pp. 91-114)
   Mach, Henryk; Volkin, David B.; Burke, Carl J.; Middaugh, C. Russell
5. Circular Dichroism (pp. 115-136)
   Kuwajima, Kunihiro
6. Infrared Spectroscopy (pp. 137-156)
   Middaugh, C. Russell; Mach, Henryk; Ryan, James A.; Sanyal, Gautam; Volkin, David B.
7. Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide Mapping (pp. 157-176)
   Williams, Kenneth R.; Stone, Kathryn L.
8. Urea and Guanidine Hydrochloride Denaturation Curves (pp. 177-190)
   Shirley, Bret A.
9. Differential Scanning Calorimetry (pp. 191-218)
   Freire, Ernesto
10. Disulfide Bonds in Protein Folding and Stability (pp. 219-252)
    Darby, Nigel; Creighton, Thomas E.
11. Solvent Stabilization of Protein Structure (pp. 253-270)
    Timasheff, Serge N.
12. Site-Directed Mutagenesis to Study Protein Folding and Stability (pp. 271-290)
    Bryan, Philip N.
13. Hydrogen Exchange Techniques (pp. 291-312)
    Scholtz, J. Martin; Robertson, Andrew D.
14. Protein Folding Kinetics (pp. 313-342)
    Kiefhaber, Thomas
15. Molten Globules (pp. 343-360)
    Fink, Anthony L.
16. Chaperonin-Assisted Protein Folding of the Enzyme Rhodanese by GroEL/GroES (pp. 361-368)
    Horowitz, Paul M.

This entry was posted on Friday, February 9th, 2007 at 3:06 pm and is filed under BioLibrary, Molecular Biology. You can follow any responses to this entry through the RSS 2.0 feed. You can leave a response, or trackback from your own site.