Stabilization of Protein Structure -- Protein Stabilization by Naturally Occurring Osmolytes -- TheThermodynamic Linkage Between Protein Structure, Stability, and Function -- Measuring the Conformational Stability of a Protein by Hydrogen Exchange -- Modeling the Native State Ensemble -- Conformational Entropy in Protein Folding -- Turn Scanning -- Laser Temperature-Jump Methods for Studying Folding Dynamics -- Kinetics of Conformational Fluctuations by EX1 Hydrogen Exchange in Native Proteins -- Molecular Dynamics Simulations of Protein Unfolding/Folding.

With the huge increase in available data on the DNA sequences of proteins, there is a growing need to understand and characterize how proteins fold into their biologically active native states and the basis for the stability of these states. In Protein Structure, Stability, and Folding, Kenneth P. Murphy and a panel of internationally recognized investigators describe some of the newest experimental and theoretical methods for investigating these critical events and processes. Among the techniques discussed are the many methods for calculating aspects of protein stability and dynamics from knowledge of the structure, for calculating conformational entropy, and for performing molecular dynamics simulations of protein unfolding. New experimental approaches presented include the use of co-solvents, novel applications of hydrogen exchange techniques, temperature-jump methods for looking at folding events, and new strategies for mutagenesis experiments. Unique in its powerful combination of theory and practice, Protein Structure, Stability, and Folding offers protein and biophysical chemists the means to gain a more comprehensive understanding of this complex area by detailing many of the major innovative techniques in use today.