From Book News, Inc.

Ten papers describe some of the newest experimental and theoretical methods for investigating protein structure, stability, and folding. Among the techniques discussed are the many methods for calculating protein stability dynamics from knowledge of the structure, and for performing molecular dynamics simulations of protein unfolding. New experimental approaches include the use of co-solvents, applications of hydrogen exchange techniques, temperature-jump methods, and mutagenesis experiments. The theory behind each experimental approach is emphasized.


Book Info

Univ. of Iowa, Iowa City. Offers protein and biophysical chemists a resource for gaining a way to understand and characterize the basis for the stability of the biologically active native states of proteins. Details major innovative techniques in use and emphasizes the theory behind each experimental approach.

Preface v
Contributors ix
1 Stabilization of Protein Structure 1
2 Protein Stabilization by Naturally Occurring Osmolytes 17
3 The Thermodynamic Linkage Between Protein Structure, Stability, and Function 37
4 Measuring the Conformational Stability of a Protein by Hydrogen Exchange 69
5 Modeling the Native State Ensemble 93
6 Conformational Entropy in Protein Folding: A Guide to Estimating Conformational Entropy via Modeling and Computation 117
7 Turn Scanning: Experimental and Theoretical Approaches to the Role of Turns 133
8 Laser Temperature-Jump Methods for Studying Folding Dynamics 159
9 Kinetics of Conformational Fluctuations by EX1 Hydrogen Exchange in Native Proteins 193
10 Molecular Dynamics Simulations of Protein Unfolding/Folding 215
Index 249